953 results match your criteria Biomolecular Nmr Assignments[Journal]


Backbone and sidechain resonance assignments and secondary structure of Scc4 from Chlamydia trachomatis.

Biomol NMR Assign 2020 Jul 2. Epub 2020 Jul 2.

Department of Chemistry, Louisiana State University, Baton Range, LA, 70803, USA.

Chlamydia trachomatis is an obligate intracellular bacterium that causes the most common sexually transmitted bacterial diseases in the world. With a biphasic developmental cycle, the bacteria utilize a type III secretion system (T3SS) to invade host cells as infectious elemental bodies, which then differentiate into actively dividing reticulate bodies. The regulation of the developmental cycle and the T3SS are linked by the bi-functional protein, specific Chlamydia chaperone 4 (Scc4). Read More

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http://dx.doi.org/10.1007/s12104-020-09965-4DOI Listing

Resonance assignment of the outer membrane protein AlkL in lipid bilayers by proton-detected solid-state NMR.

Biomol NMR Assign 2020 Jun 30. Epub 2020 Jun 30.

Centre de RMN à Très Hauts Champs de Lyon (FRE 2034 - CNRS, UCB Lyon 1, ENS Lyon), Université de Lyon, 5 rue de la Doua, 69100, Villeurbanne, France.

Most commonly small outer membrane proteins, possessing between 8 and 12 β-strands, are not involved in transport but fulfill diverse functions such as cell adhesion or binding of ligands. An intriguing exception are the 8-stranded β-barrel proteins of the OmpW family, which are implicated in the transport of small molecules. A representative example is AlkL from Pseudomonas putida GPoI, which functions as a passive importer of hydrophobic molecules. Read More

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http://dx.doi.org/10.1007/s12104-020-09964-5DOI Listing

H, C and N backbone resonance assignment of BRCA1 fragment 219-504.

Biomol NMR Assign 2020 Jun 24. Epub 2020 Jun 24.

Faculty of Chemistry, Institute of Biological Chemistry, University Vienna, Währinger Straße 38, 1090, Vienna, Austria.

The breast cancer susceptibility protein 1 (BRCA1) plays a central role in the suppression of human breast and ovarian cancer. Germ line mutations of the BRCA1 gene are responsible for the hereditary breast and ovarian cancer (HBOC) syndrome. Here were report H, C, and N resonance assignments for the intrinsically disordered BRCA1 fragment 219-504, which contains important interaction sites for the proto-oncogenic transcription factor MYC as well as for p53. Read More

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http://dx.doi.org/10.1007/s12104-020-09963-6DOI Listing

NMR resonance assignments of the programmed cell death protein 5 (PDCD5) from Toxoplasma gondii.

Biomol NMR Assign 2020 Jun 23. Epub 2020 Jun 23.

Genome and Systems Biology Degree Program, National Taiwan University and Academia Sinica, Taipei, Taiwan.

Toxoplasmosis is a systematic protozoan disease caused by a tiny parasite Toxoplasma gondii. The infection can be dangerous for pregnant woman and people with weak immune systems. The secreted protein named TgPDCD5 (Programmed cell death protein 5 from Toxoplasma gondii) plays an important role in apoptosis-inducing effect on host cells. Read More

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http://dx.doi.org/10.1007/s12104-020-09961-8DOI Listing

Backbone resonance assignment and dynamics of 110 kDa hexameric inorganic pyrophosphatase from Mycobacterium tuberculosis.

Biomol NMR Assign 2020 Jun 19. Epub 2020 Jun 19.

Center for Magnetic Tomography and Spectroscopy, Faculty of Fundamental Medicine, M.V. Lomonosov Moscow State University, 119991, Moscow, Russia.

Family I soluble inorganic pyrophosphatases (PPases; EC 3.6.1. Read More

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http://dx.doi.org/10.1007/s12104-020-09962-7DOI Listing

H, C, N backbone and IVL methyl group resonance assignment of the fungal β-glucosidase from Trichoderma reesei.

Biomol NMR Assign 2020 Jun 19. Epub 2020 Jun 19.

YSBL, Department of Chemistry, University of York, Heslington, York, UK.

β-glucosidases have received considerable attention due to their essential role in bioethanol production from lignocellulosic biomass. β-glucosidase can hydrolyse cellobiose in cellulose degradation and its low activity has been considered as one of the main limiting steps in the process. Large-scale conversions of cellulose therefore require high enzyme concentration which increases the cost. Read More

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http://dx.doi.org/10.1007/s12104-020-09959-2DOI Listing

H, C, and N backbone assignments of the C-terminal region of the human retinoic acid-induced protein 2.

Biomol NMR Assign 2020 Jun 18. Epub 2020 Jun 18.

Leibniz Institute on Aging - Fritz Lipmann Institute, Beutenbergstr. 11, 07745, Jena, Germany.

Retinoic acid-induced protein 2 is a human protein of 530 residues encoded by the RAI2 gene (Q9Y5P3; RAI2_HUMAN). RAI2 is a novel tumor suppressor protein whose depletion in breast cancer cell lines results in the downregulation of several genes associated with differentiation along with increased invasiveness and aggressive tumor phenotype of the cells. The role of the protein is specified to be a transcriptional regulator that promotes chromosomal stability and hence controls the expression of several regulators of cancer and metastasis. Read More

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http://dx.doi.org/10.1007/s12104-020-09960-9DOI Listing

Backbone resonance assignments of the catalytic and regulatory domains of Ca/calmodulin-dependent protein kinase 1D.

Biomol NMR Assign 2020 Jun 13. Epub 2020 Jun 13.

Department of Biochemistry, University of Alberta, Edmonton, AB, T6G 2H7, Canada.

The CaMK subfamily of Ser/Thr kinases are regulated by calmodulin interactions with their C-terminal regions. They are exemplified by Ca/calmodulin dependent protein kinase 1δ which is known as CaMK1D, CaMKIδ or CKLiK. CaMK1D mediates intracellular signalling downstream of Ca influx and thereby exhibits amplifications of Casignals and polymorphisms that have been implicated in breast cancer and diabetes. Read More

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http://dx.doi.org/10.1007/s12104-020-09950-xDOI Listing

H, C, and N backbone chemical shift assignments of mGTP cap-bound Leishmania initiation factor 4E-1.

Biomol NMR Assign 2020 Jun 9. Epub 2020 Jun 9.

Department of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA, 02115, USA.

Most of the translational control of gene expression in higher eukaryotes occurs during the initiation step of protein synthesis. While this process is well characterized in mammalian cells, it is less defined in parasites, including the ones that cause human Leishmaniasis. The Leishmania cap-binding isoform 1 (LeishIF4E-1) is the only isoform that binds the specific trypanosomatids-specific hypermethylated 5' cap, called cap-4, in the human stage of the parasite life cycle. Read More

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http://dx.doi.org/10.1007/s12104-020-09958-3DOI Listing

Backbone and side-chain chemical shift assignments of a cellular FLICE-inhibitory protein (c-FLIP).

Biomol NMR Assign 2020 Jun 6. Epub 2020 Jun 6.

State Key Laboratory of Phytochemistry and Plant Resources in West China, Kunming Institute of Botany, Chinese Academy of Sciences, 132 Lanhei Road, Heilongtan, Kunming, 650201, Yunnan, People's Republic of China.

Cellular FLICE-inhibitory protein (c-FLIP), which is involved in regulating the apoptosis of the extrinsic cell death pathway contains two death effector domains (DED). There are several splicing variants including short-form (c-FLIP) and long-form (c-FLIP). The death-inducing signaling complex (DISC) initiates apoptosis and programmed necrosis, DISC assembly and activation are regulated by c-FLIP. Read More

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http://dx.doi.org/10.1007/s12104-020-09953-8DOI Listing

H, C and  N NMR assignments of solubility tag protein Msyb of Escherichia coli.

Biomol NMR Assign 2020 Jun 5. Epub 2020 Jun 5.

BioBank, First Affiliated Hospital of Xi'an Jiaotong University, Shaanxi, 710061, China.

Biochemical and structural characterizations of a protein are the prerequisite for the further understanding of its biological role and potential applications. The expression of recombinant protein is almost unavoidable to produce the amount of the protein required for these studies, especially at the industrial level. Escherichia coli is the single most used system for recombinant protein expression and the first choice for a trial expression. Read More

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http://dx.doi.org/10.1007/s12104-020-09955-6DOI Listing

H, N and C resonance assignments of the HR1c domain of PRK1, a protein kinase C-related kinase.

Biomol NMR Assign 2020 Jun 4. Epub 2020 Jun 4.

Department of Biochemistry, 80, Tennis Court Road, Cambridge, CB2 1GA, UK.

PRK1 is a member of the protein kinase C-related kinase (PRK) family of serine/threonine kinases and a downstream effector of Rho GTPases. PRK1 has three N-terminal Homology Region 1 (HR1) domains (HR1a, HR1b and HR1c), which form antiparallel coiled coils that interact with Rho family GTPases. PRK1 also has a C2-like domain that targets it to the plasma membrane and a kinase domain, which is a member of the protein kinase C superfamily. Read More

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http://dx.doi.org/10.1007/s12104-020-09954-7DOI Listing

H, C, N backbone resonance assignments of the apo and holo forms of the ABC transporter solute binding protein PiuA from Streptococcus pneumoniae.

Biomol NMR Assign 2020 Jun 3. Epub 2020 Jun 3.

Department of Chemistry, Indiana University, Bloomington, Indiana, USA.

Streptococcus pneumoniae is a Gram-positive human pathogen that causes millions of infections worldwide with an increasing occurrence of antibiotic resistance. Iron acquisition is essential for its survival and virulence, especially under host-imposed nutritional immunity. S. Read More

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http://dx.doi.org/10.1007/s12104-020-09952-9DOI Listing

H, C and N resonance assignments of Q38FZ4, hypothetical protein from Trypanosoma brucei.

Biomol NMR Assign 2020 Jun 3. Epub 2020 Jun 3.

Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, 230026, Anhui, People's Republic of China.

Q38FZ4 (UniProt accession number), is an 85-residue hypothetical protein from Trypanosoma brucei (T. brucei). Q38FZ4, which might be specific among the trypanosomatid genomes, shares low sequence similarity with mammal proteins and also has an essential function in the growth of T. Read More

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http://dx.doi.org/10.1007/s12104-020-09956-5DOI Listing

H, C and N NMR chemical shift assignments of cAMP-regulated phosphoprotein-19 and -16 (ARPP-19 and ARPP-16).

Biomol NMR Assign 2020 May 28. Epub 2020 May 28.

Department of Biological and Environmental Science, University of Jyvaskyla, Jyvaskyla, Finland.

Protein Phosphatase 2A, PP2A, the principal Serine/threonine phosphatase, has major roles in broad range of signaling pathways that include regulation of cell cycle, cell proliferation and neuronal signaling. The loss of function of PP2A is linked with many human diseases, like cancer and neurodegenerative disorders. Protein phosphatase 2A (PP2A) functions as tumor suppressor and its tumor suppressor activity is inhibited by the overexpression of PP2A inhibitor proteins in most of the cancers. Read More

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http://dx.doi.org/10.1007/s12104-020-09951-wDOI Listing

Resonance assignments and secondary structure prediction of secretory protein Rv0603 from Mycobacterium tuberculosis H37Rv.

Biomol NMR Assign 2020 May 20. Epub 2020 May 20.

Molecular and Structural Biology Division, CSIR-Central Drug Research Institute, Lucknow, Uttar Pradesh, 226 031, India.

We report the NMR resonance assignments of N-terminal signal sequence deleted secretory protein Rv0603 (∆-Rv0603) from Mycobacterium tuberculosis H37Rv. ∆-Rv0603 displayed good peak yield and signal dispersion in 2D [N-H] HSQC spectrum, which prompted us to proceed for resonance assignments on this construct. Standard triple-resonance experiments for resonance assignments were recorded on [U-N]-∆Rv0603 and [U-N, C]-∆Rv0603 samples. Read More

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http://dx.doi.org/10.1007/s12104-020-09948-5DOI Listing

H, C and N assignment of the paramagnetic high potential iron-sulfur protein (HiPIP) PioC from Rhodopseudomonas palustris TIE-1.

Biomol NMR Assign 2020 May 15. Epub 2020 May 15.

Magnetic Resonance Center (CERM), Department of Chemistry and Consorzio Interuniversitario Risonanze Magnetiche Metallo Proteine (C.I.R.M.M.P.), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.

High potential iron-sulfur proteins (HiPIPs) are a class of small proteins (50-100 aa residues), containing a 4Fe-4S iron-sulfur cluster. The 4Fe-4S cluster shuttles between the oxidation states [FeS], with a positive redox potential in the range (500-50 mV) throughout the different known HiPIPs. Both oxidation states are paramagnetic at room temperature. Read More

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http://dx.doi.org/10.1007/s12104-020-09947-6DOI Listing

H, C and N resonance assignments of TFIIS LW domain from Homo sapiens.

Biomol NMR Assign 2020 May 2. Epub 2020 May 2.

Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, Anhui, 230027, Hefei, China.

LW domain is the N-terminal domain I of transcription elongation factor TFIIS, which is a component of RNA polymerase II (Pol II) preinitiation complexes (PICs). Here, we report the resonance assignments of TFIIS LW domain from Homo sapiens for further understanding of the relationship between its structure and function. Read More

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http://dx.doi.org/10.1007/s12104-020-09945-8DOI Listing

H, C, N resonance assignments and secondary structure of yeast oligosaccharyltransferase subunit Ost4 and its functionally important mutant Ost4V23D.

Biomol NMR Assign 2020 Apr 23. Epub 2020 Apr 23.

Department of Chemistry, Oklahoma State University, 74078, Stillwater, OK, USA.

Asparagine-linked glycosylation is an essential and highly conserved protein modification reaction that occurs in the endoplasmic reticulum of cells during protein synthesis at the ribosome. In the central reaction, a pre-assembled high-mannose sugar is transferred from a lipid-linked donor substrate to the side-chain of an asparagine residue in an -N-X-T/S- sequence (where X is any residue except proline). This reaction is carried by a membrane-bound multi-subunit enzyme complex, oligosaccharyltransferase (OST). Read More

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http://dx.doi.org/10.1007/s12104-020-09946-7DOI Listing

Assigned NMR backbone resonances of the ligand-binding region domain of the pneumococcal serine-rich repeat protein (PsrP-BR) reveal a rigid monomer in solution.

Biomol NMR Assign 2020 Apr 20. Epub 2020 Apr 20.

Department of Molecular Sciences, Swedish University of Agricultural Sciences, PO Box 7015, 750 07, Uppsala, Sweden.

The pneumococcal serine rich repeat protein (PsrP) is displayed on the surface of Streptococcus pneumoniae with a suggested role in colonization in the human upper respiratory tract. Full-length PsrP is a 4000 residue-long multi-domain protein comprising a positively charged functional binding region (BR) domain for interaction with keratin and extracellular DNA during pneumococcal adhesion and biofilm formation, respectively. The previously determined crystal structure of the BR domain revealed a flat compressed barrel comprising two sides with an extended β-sheet on one side, and another β-sheet that is distorted by loops and β-turns on the other side. Read More

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http://dx.doi.org/10.1007/s12104-020-09944-9DOI Listing

Backbone and sidechain NMR assignments for the ribosome maturation factor RimP from Escherichia coli.

Biomol NMR Assign 2020 Apr 17. Epub 2020 Apr 17.

Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801A, 48160, Derio, Bizkaia, Spain.

Ribosome biogenesis is an energetically expensive and complex cellular process that involves the coordinated folding of the ribosomal RNA and dozens of ribosomal proteins. It proceeds along multiple parallel pathways and is guided by trans-acting factors called ribosome assembly factors. Although this process has been studied for decades, there are still many open questions regarding the role of the ribosome assembly factors in directing the folding of ribosome biogenesis intermediates. Read More

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http://dx.doi.org/10.1007/s12104-020-09943-wDOI Listing

Correction to: H, C, and N resonance assignments of human calmodulin bound to a peptide derived from the STRA6 vitamin A transporter (CaMBP2).

Biomol NMR Assign 2020 Apr 4. Epub 2020 Apr 4.

Department of Biochemistry and Molecular Biology, Center for Biomolecular Therapeutics (CBT), University of Maryland School of Medicine, 108 N. Greene St., Baltimore, MD, 21201, USA.

The article H, C, and N resonance assignments of human calmodulin bound to a peptide derived from the STRA6 vitamin A transporter (CaMBP2), written by Kristen M. Varney, Paul T. Wilder, Raquel Godoy-Ruiz, Filippo Mancia and David J. Read More

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http://dx.doi.org/10.1007/s12104-020-09942-xDOI Listing

H, C, and N Backbone assignments of the human brain and acute leukemia cytoplasmic (BAALC) protein.

Biomol NMR Assign 2020 Apr 2. Epub 2020 Apr 2.

Institute of Biochemistry and Biotechnology, Charles Tanford Protein Center, Martin-Luther-University Halle-Wittenberg, Kurt-Mothes-Str. 3a, 06120, Halle, Germany.

The brain and acute leukemia cytoplasmic (BAALC; UniProt entry Q8WXS3) is a 180-residue-long human protein having six known isoforms. BAALC is expressed in either hematopoietic or neuroectodermal cells and its specific function is still to be revealed. However, as a presumably membrane-anchored protein at the cytoplasmic side it is speculated that BAALC exerts its function at the postsynaptic densities of certain neurons and might play a role in developing cytogenetically normal acute myeloid leukemia (CN-AML) when it is highly overexpressed by myeloid or lymphoid progenitor cells. Read More

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http://dx.doi.org/10.1007/s12104-020-09938-7DOI Listing

H, N chemical shift assignments of the imino groups of yeast tRNA: influence of the post-transcriptional modifications.

Biomol NMR Assign 2020 Apr 1. Epub 2020 Apr 1.

Expression Génétique Microbienne, UMR 8261, CNRS, Université de Paris, Institut de Biologie Physico-Chimique (IBPC), 13 rue Pierre et Marie Curie, 75005, Paris, France.

Transfer RNAs (tRNAs) are heavily decorated with post-transcriptional modifications during their biosynthesis. To fulfil their functions within cells, tRNAs undergo a tightly controlled biogenesis process leading to the formation of mature tRNAs. In particular, the introduction of post-transcriptional modifications in tRNAs is controlled and influenced by multiple factors. Read More

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http://dx.doi.org/10.1007/s12104-020-09939-6DOI Listing

H, C, N chemical shift assignments of SHP2 SH2 domains in complex with PD-1 immune-tyrosine motifs.

Biomol NMR Assign 2020 Apr 1. Epub 2020 Apr 1.

Center for Biomolecular Drug Design and Institute of Organic Chemistry, Leibniz University Hannover, Schneiderberg 38, 30167, Hannover, Germany.

Inhibition of immune checkpoint receptor Programmed Death-1 (PD-1) via monoclonal antibodies is an established anticancer immunotherapeutic approach. This treatment has been largely successful; however, its high cost demands equally effective, more affordable alternatives. To date, the development of drugs targeting downstream players in the PD-1-dependent signaling pathway has been hampered by our poor understanding of the molecular details of the intermolecular interactions involved in the pathway. Read More

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http://dx.doi.org/10.1007/s12104-020-09941-yDOI Listing

H, C, and N chemical shift assignment of human PACSIN1/syndapin I SH3 domain in solution.

Biomol NMR Assign 2020 Mar 31. Epub 2020 Mar 31.

Institut Pasteur de Lille, U1167 - RID-AGE - Risk Factors and Molecular Determinants of Aging-Related Diseases, Univ. Lille, Inserm, CHU Lille, 59000, Lille, France.

Human neuron-specific PACSIN1 plays a key role in synaptic vesicle recycling and endocytosis, as well as reorganization of the microtubule dynamics to maintain axonal plasticity. PACSIN1 contains a highly conserved C-terminal SH3 domain and an F-bar domain at its N-terminus. Due to its remarkable interaction network, PACSIN1 plays a central role in key neuronal functions. Read More

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http://dx.doi.org/10.1007/s12104-020-09940-zDOI Listing

pH-dependent secondary structure propensity of the influenza A virus M2 cytoplasmic tail.

Biomol NMR Assign 2020 04 10;14(1):157-161. Epub 2020 Mar 10.

Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.

The cytoplasmic C-terminal tail of the matrix protein 2 (M2) from influenza A virus has a well conserved sequence and is involved in interactions with several host proteins as well as the influenza matrix protein 1 (M1). Whereas the transmembrane domain of M2 has been well characterised structurally and functionally, high resolution information about the distal cytoplasmic tail is lacking. Here we report the chemical shifts of the cytoplasmic tail of M2 and the chemical shift perturbations at low pH and in the presence of membrane mimetics. Read More

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http://dx.doi.org/10.1007/s12104-020-09937-8DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7069904PMC

NMR backbone assignment of the Cε4 domain of immunoglobulin E.

Biomol NMR Assign 2020 04 27;14(1):151-155. Epub 2020 Feb 27.

Randall Centre for Cell & Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London, SE1 1UL, UK.

Immunoglobulin E (IgE) plays a central role in allergic reactions. IgE is a dynamic molecule that is capable of undergoing large conformational changes. X-ray crystal structures of the Fc region of IgE in complex with various ligands have shown that IgE-Fc can exist in extended and various bent conformations. Read More

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http://dx.doi.org/10.1007/s12104-020-09936-9DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7069932PMC

Backbone H, C and N resonance assignments of the proteasome lid subunit Rpn12 from Saccharomyces cerevisiae.

Biomol NMR Assign 2020 04 19;14(1):147-150. Epub 2020 Feb 19.

College of Life Sciences, Peking University, Beijing, 100871, China.

The 26S proteasome degrades selected polyubiquitinated proteins in the ubiquitin-proteasome system, which is the major pathway for programmed protein degradation in eukaryotic cells. The Saccharomyces cerevisiae Rpn12 locates in the lid of the 19S regulatory particle within the 26S proteasome and plays a role in recruiting the extrinsic ubiquitin receptor Rpn10. Rpn12 contains a N-terminal TPR (tetratrico peptide repeat)-like domain and a C-terminal WH (winged helix) domain. Read More

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http://dx.doi.org/10.1007/s12104-020-09935-wDOI Listing

Complete sequential assignment and secondary structure prediction of the cannulae forming protein CanA from the hyperthermophilic archaeon Pyrodictium abyssi.

Biomol NMR Assign 2020 04 12;14(1):141-146. Epub 2020 Feb 12.

Institute of Biophysics and Physical Biochemistry, Biophysics I and Centre of Magnetic Resonance in Chemistry and Biomedicine (CMRCB), University of Regensburg, Universitätsstr. 31, 93053, Regensburg, Germany.

CanA from Pyrodictium abyssi forms a heat-resistant organic hollow-fiber network together with CanB and CanC. An N-terminally truncated construct of CanA (K-CanA) gave NMR spectra of good quality that could be assigned by three-dimensional NMR methods on N and C-N enriched protein. We assigned the chemical shifts of 96% of all backbone H atoms, 98% of all backbone N atoms, 100% of all C atoms, 100% of all H atoms, 90% of all C' atoms, and 100% of the C atoms. Read More

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http://dx.doi.org/10.1007/s12104-020-09934-xDOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7069910PMC

Box C/D snoRNPs: solid-state NMR fingerprint of an early-stage 50 kDa assembly intermediate.

Biomol NMR Assign 2020 04 6;14(1):131-140. Epub 2020 Feb 6.

CRM2, UMR 7036 CNRS, Université de Lorraine, Faculté des Sciences et Technologies, Nancy, France.

Many cellular functions rely on stable protein-only or protein-RNA complexes. Deciphering their assembly mechanism is a key question in cell biology. We here focus on box C/D small nucleolar ribonucleoproteins involved in ribosome biogenesis. Read More

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http://dx.doi.org/10.1007/s12104-020-09933-yDOI Listing

Backbone assignment of ribose-5-phosphate isomerase of Mycobacterium tuberculosis (MtRpiB).

Biomol NMR Assign 2020 04 6;14(1):119-122. Epub 2020 Feb 6.

Institute of Medical Biochemistry (IBqM), National Center of Nuclear Magnetic Resonance Jiri Jonas, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil.

Tuberculosis is one of the deadliest diseases worldwide affecting approximately 10 million people in 2018. This classifies tuberculosis as epidemic in several countries and leads to an increasing number of multidrug-resistant strains. Thus, the development of new drugs is essential to effective treatments. Read More

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http://dx.doi.org/10.1007/s12104-020-09931-0DOI Listing

Complete assignment of Ala, Ile, Leu, Met and Val methyl groups of the protruding domain from human norovirus GII.4 Saga.

Biomol NMR Assign 2020 04 28;14(1):123-130. Epub 2020 Jan 28.

Center of Structural and Cell Biology in Medicine (CSCM), Institute of Chemistry and Metabolomics, University of Lübeck, Ratzeburger Allee 160, 23562, Lübeck, Germany.

Attachment of human noroviruses to histo blood group antigens (HBGAs) is thought to be essential for infection, although how this binding event promotes infection is unknown. Recent studies have shown that 60% of all GII.4 epidemic strains may undergo a spontaneous post-translational modification (PTM) in an amino acid located adjacent to the binding pocket for HBGAs. Read More

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http://dx.doi.org/10.1007/s12104-020-09932-zDOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7069894PMC

H, C, and N resonance assignment and secondary structure of the pheromone-binding protein2 from the agricultural pest Ostrinia furnacalis (OfurPBP2).

Biomol NMR Assign 2020 04 23;14(1):115-118. Epub 2020 Jan 23.

Oklahoma State University Stillwater, Stillwater, OK, USA.

Ostrinia furnacalis, a lepidopteran moth, is an invasive pest found in Asia, Australia, Africa, and parts of the United States. The O. furnacalis pheromone-binding protein2 (OfurPBP2), present in the male moth antenna, plays a role in the detection of female-secreted pheromone in a process that leads to mating. Read More

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http://dx.doi.org/10.1007/s12104-020-09930-1DOI Listing

H, C,  N chemical shift assignments of the FKBP12 protein from the pathogenic fungi Candida auris and Candida glabrata.

Biomol NMR Assign 2020 04 16;14(1):105-109. Epub 2020 Jan 16.

Wadsworth Center, New York State Department of Health, Empire State Plaza, Albany, NY, 12201, USA.

Multi-drug resistance is becoming an increasingly severe clinical challenge not only among pathogenic bacteria but among fungal pathogens as well. Drug design is inherently more challenging for the eukaryotic fungi due to their closer evolutionary similarity to humans. The recent rapid expansion in invasive infections throughout the world by Candida auris is of particular concern due to a substantial mortality rate, comparatively facile transmission, and an increasing level of resistance to all three of the major classes of anti-fungal drugs. Read More

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http://dx.doi.org/10.1007/s12104-020-09928-9DOI Listing

Resonance assignments of bacteriophage SPO1 Gp49 protein.

Biomol NMR Assign 2020 04 14;14(1):111-114. Epub 2020 Jan 14.

BioBank, First Affiliated Hospital, School of Medicine, Xi'an Jiaotong University, Xi'an, 710061, Shaanxi, China.

Recent applications of phage therapy in localized wound and drug-resistant bacterial infection have brought bacteriophage back to the spotlight. While these works demonstrated the safety and effectiveness of engineered bacteriophages in human patients, the exact molecular machinery behind the bacteria killing remains largely uncharacterized. This is particularly noticable outside Escherichia coli phages, as most studies are based on bacteriophages of this Gram-negative model bacterium. Read More

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http://dx.doi.org/10.1007/s12104-020-09929-8DOI Listing

NMR resonance assignments for the active and inactive conformations of the small G protein RalA.

Biomol NMR Assign 2020 04 8;14(1):87-91. Epub 2020 Jan 8.

Department of Biochemistry, 80, Tennis Court Road, Cambridge, CB2 1GA, UK.

The Ral proteins (RalA and RalB) are small G proteins of the Ras family that have been implicated in exocytosis, endocytosis, transcriptional regulation and mitochondrial fission, as well as having a role in tumourigenesis. RalA and RalB are activated downstream of the master regulator, Ras, which causes the nucleotide exchange of GDP for GTP. Here we report the H,  N and C resonance assignments of RalA in its active form bound to the GTP analogue GMPPNP. Read More

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http://dx.doi.org/10.1007/s12104-019-09925-7DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7069931PMC

Solid-state NMR C, N assignments of human histone H3 in the nucleosome core particle.

Biomol NMR Assign 2020 04 6;14(1):99-104. Epub 2020 Jan 6.

School of Biological Sciences, Nanyang Technological University, Singapore, 637551, Singapore.

Nucleosome core particle (NCP), the basic unit of chromatin in eukaryotic cells, consists of ~ 147 bp DNA wrapped around a histone octamer (HO) formed by two H2A-H2B dimers and one (H3-H4) tetramer. Histones undergo various post-translational modifications (PTMs), which regulates genomic activities in different cellular phases. High-resolution structures have been solved for many nucleosomes primarily including NCPs. Read More

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http://dx.doi.org/10.1007/s12104-020-09927-wDOI Listing

H, C and N resonance assignments of translation initiation factor 3 from Pseudomonas aeruginosa.

Biomol NMR Assign 2020 04 4;14(1):93-97. Epub 2020 Jan 4.

Department of Chemistry, The University of Texas Rio Grande Valley, Edinburg, TX, 78539, USA.

Translation initiation factor 3 (IF3) is one of the three protein factors that bind to the small ribosomal subunit and it is required for the initiation of protein biosynthesis in bacteria. IF3 contains two independent domains, N- and C-terminal domains, which are connected by a lysine-rich interdomain linker. IF3 undergoes large-scale movements and conformational changes upon binding to the 30S subunit and also during the functional regulation of initiation. Read More

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http://dx.doi.org/10.1007/s12104-020-09926-xDOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7073282PMC

H, C and N backbone resonance assignment of the human BRCA2 N-terminal region.

Biomol NMR Assign 2020 04 3;14(1):79-85. Epub 2020 Jan 3.

Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ Paris-Sud, Université Paris-Saclay, Gif-sur-Yvette Cedex, France.

The Breast Cancer susceptibility protein 2 (BRCA2) is involved in mechanisms that maintain genome stability, including DNA repair, replication and cell division. These functions are ensured by the folded C-terminal DNA binding domain of BRCA2 but also by its large regions predicted to be disordered. Several studies have shown that disordered regions of BRCA2 are subjected to phosphorylation, thus regulating BRCA2 interactions through the cell cycle. Read More

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http://dx.doi.org/10.1007/s12104-019-09924-8DOI Listing

NMR assignments of protrusion domain of capsid protein from dragon grouper nervous necrosis virus.

Biomol NMR Assign 2020 04 17;14(1):63-66. Epub 2019 Dec 17.

Institute of Chemistry, Academia Sinica, Nankang, Taipei, 11529, Taiwan, ROC.

Nervous necrosis virus (NNV) is a non-enveloped virus that causes massive mortality in aquaculture fish production worldwide. Recently X-ray crystallography and single particle cryo-EM have independently determined the icosahedral capsid of NNV to near-atomic resolutions to show the capsid protein is composed of a S-domain (shell) and a P-domain (protrusion) connected by a linker. However, the structure of the spike on NNV capsid made of trimeric P-domains was poorly resolved by cryo-EM. Read More

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http://dx.doi.org/10.1007/s12104-019-09921-xDOI Listing

H, C, N backbone and side-chain resonance assignment of the native form of UbcH7 (UBE2L3) through solution NMR spectroscopy.

Biomol NMR Assign 2020 04 2;14(1):73-78. Epub 2019 Dec 2.

Department of Pharmacy, University of Patras, 26504, Patras, Greece.

Ubiquitination is a post-translational modification that regulates a plethora of processes in cells. Ubiquitination requires three type of enzyme: E1 ubiquitin (Ub) activating enzymes, E2 Ub conjugating enzymes and E3 ubiquitin ligases. The E2 enzymes perform a variety of functions, as Ub chain initiation, elongation and regulation of the topology and the process of chain formation. Read More

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http://dx.doi.org/10.1007/s12104-019-09923-9DOI Listing

NMR assignments of a dynamically perturbed and dimerization inhibited N-terminal domain variant of a spider silk protein from E. australis.

Biomol NMR Assign 2020 04 30;14(1):67-71. Epub 2019 Nov 30.

Institute for Pharmacy and Biochemistry, Johannes-Gutenberg-University Mainz, Johann-Joachim Becher-Weg 30, 55128, Mainz, Germany.

Web spiders use specialized glands to produce silk proteins, so-called spidroins, which assemble into extraordinarily tough silk fibers through tightly regulated phase and structural transitions. A crucial step in the polymerization of spidroins is the pH-triggered assembly of their N-terminal domains (NTDs) into tight dimers. Major ampullate spidroin NTDs contain an unusually high content of the amino acid methionine. Read More

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http://dx.doi.org/10.1007/s12104-019-09922-wDOI Listing

Backbone and side-chain chemical shift assignments for the ribosome-inactivating protein trichobakin (TBK).

Biomol NMR Assign 2020 04 16;14(1):55-61. Epub 2019 Nov 16.

Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.

Trichobakin (TBK) is a type-I ribosome-inactivating protein (RIP-I), acting as an extremely potent inhibitor of protein synthesis in the cell-free translation system of rabbit reticulocyte lysate (IC: 3.5 pM). In this respect, TBK surpasses the well-studied highly homologous RIP-I trichosanthin (IC: 20-27 pM), therefore creation of recombinant toxins based on it is of great interest. Read More

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http://dx.doi.org/10.1007/s12104-019-09920-yDOI Listing

Resonance assignments of bacteriophage T4 Y04L protein.

Biomol NMR Assign 2020 04 9;14(1):51-54. Epub 2019 Nov 9.

BioBank, First Affiliated Hospital, School of Medicine, Xi'an Jiaotong University, Xi'an, 710061, Shaanxi, China.

Phage study draws more attention recently as the bacterial antibiotic resistances become a major threat for global health. Bacteriophage T4 is one of the most studied the phages and the representative of Tevenvirinae subfamily. Since 1950s, T4 phage has been studied more intensively than any other large lytic phages and its biological studies have provided basis for current phage biology as well as other applications. Read More

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http://dx.doi.org/10.1007/s12104-019-09919-5DOI Listing

NMR resonance assignments of the four isoforms of the hazelnut allergen Cor a 1.04.

Biomol NMR Assign 2020 04 5;14(1):45-49. Epub 2019 Nov 5.

Institute of Organic Chemistry, Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck, Innrain 80/82, 6020, Innsbruck, Austria.

In large parts of Europe, Northern America and China people are suffering from allergies after consuming certain kinds of fruits and vegetables. Typical allergic symptoms range from scratching and itching of the throat to severe symptoms like rhino conjunctivitis and anaphylaxis. For hazelnuts (Corylus avellana), these allergies result from initial sensitization to the birch (Betula verrucosa) pollen allergen Bet v 1 and subsequent development of allergic cross-reactions to proteins that are similar in their three-dimensional structure to the sensitizing protein Bet v 1. Read More

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http://dx.doi.org/10.1007/s12104-019-09918-6DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7069924PMC
April 2020
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Backbone and side chain H, N and C chemical shift assignments of the molten globule state of L94G mutant of horse cytochrome-c.

Biomol NMR Assign 2020 04 4;14(1):37-44. Epub 2019 Nov 4.

NMR-II Lab, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi, 110067, India.

Proteins fold via a number of intermediates that help them to attain their unique native 3D structure. These intermediates can be trapped under extreme conditions of pH, temperature and chemical denaturants. Similar states can also be achieved by other processes like chemical modification, site directed mutagenesis (or point mutation) and cleavage of covalent bonds of natural proteins under physiological conditions usually taken as dilute buffer (near neutral pH) and 25 °C. Read More

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http://dx.doi.org/10.1007/s12104-019-09917-7DOI Listing

H, C, and N backbone and side chain chemical shift assignment of YdaS, a monomeric member of the HigA family.

Biomol NMR Assign 2020 04 17;14(1):25-30. Epub 2019 Oct 17.

Structural Biology Brussels, Department of Biotechnology (DBIT), Vrije Universiteit Brussel, Brussels, Belgium.

The cryptic prophage CP-933P in Escherichia coli O157:H7 contains a parDE-like toxin-antitoxin module, the operator region of which is recognized by two flanking transcription regulators: PaaR2 (ParE associated Regulator), which forms part of the paaR2-paaA2-parE2 toxin-antitoxin operon and YdaS (COG4197), which is encoded in the opposite direction but shares the operator. Here we report the H, N and C backbone and side chain chemical shift assignments of YdaS from Escherichia coli O157:H7 in its free state. YdaS is a distinct relative to HigA antitoxins but behaves as a monomer in solution. Read More

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http://dx.doi.org/10.1007/s12104-019-09915-9DOI Listing

Backbone, side chain and heme resonance assignment of the triheme cytochrome PpcA from Geobacter metallireducens in the oxidized state.

Biomol NMR Assign 2020 04 15;14(1):31-36. Epub 2019 Oct 15.

UCIBIO-Requimte, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade NOVA de Lisboa, Campus Caparica, 2829-516, Caparica, Portugal.

The bacterium Geobacter metallireducens is capable of transferring electrons to the cell exterior, a process designated extracellular electron transfer. This mechanism allows the microorganism to reduce extracellular acceptors such as Fe(III) (hydr)oxides and water toxic and/or radioactive contaminants including Cr(VI) and U(VI). It is also capable of oxidizing waste water aromatic organic compounds being an important microorganism for bioremediation of polluted waters. Read More

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http://dx.doi.org/10.1007/s12104-019-09916-8DOI Listing

NMR chemical shift assignment of a constitutively active fragment of the antitermination protein LicT.

Biomol NMR Assign 2020 04 14;14(1):19-23. Epub 2019 Oct 14.

Centre de Biochimie Structurale (CBS), INSERM, CNRS, Univ Montpellier, Montpellier, France.

LicT belongs to an essential family of bacterial antitermination proteins which bind to nascent mRNAs in order to stimulate transcription of sugar-metabolizing operons. As most of other antitermination proteins involved in carbohydrate metabolism, LicT is composed of a N-terminal RNA-binding module (CAT) and two homologous regulatory modules (PRD1 and PRD2). The activity of the CAT effector module is controlled by antagonist phosphorylations by the phosphotransferase system on conserved histidines of the two C-terminal PRDs in response to available carbon sources. Read More

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http://dx.doi.org/10.1007/s12104-019-09914-wDOI Listing