Structural basis of severe acute respiratory syndrome coronavirus ADP-ribose-1'-phosphate dephosphorylation by a conserved domain of nsP3
| العنوان: | Structural basis of severe acute respiratory syndrome coronavirus ADP-ribose-1'-phosphate dephosphorylation by a conserved domain of nsP3 |
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| المؤلفون: | Tom Clayton, Raymond C. Stevens, Mark T. Griffith, Vanitha Subramanian, Benjamin W. Neuman, Michael J. Buchmeier, Jeremiah S. Joseph, Kin Moy, Peter Kuhn, Jeffrey Velasquez, Kumar Singh Saikatendu |
| المصدر: | Structure (London, England : 1993) Structure (London, England : 1993), vol 13, iss 11 |
| سنة النشر: | 2005 |
| مصطلحات موضوعية: | Protein Structure, Sequence analysis, Protein domain, Phosphatase, Molecular Sequence Data, Biophysics, Biology, Viral Nonstructural Proteins, Article, Dephosphorylation, Macro domain, Structure-Activity Relationship, Protein structure, Structural Biology, Sequence Analysis, Protein, Information and Computing Sciences, Amino Acid Sequence, Phosphorylation, Peptide sequence, Molecular Biology, Conserved Sequence, Adenosine Diphosphate Ribose, Protein, RNA, Biological Sciences, SARS Virus, RNA-Dependent RNA Polymerase, Protein Structure, Tertiary, RNA Replicase, Biochemistry, Severe acute respiratory syndrome-related coronavirus, Chemical Sciences, Sequence Analysis, Tertiary |
| الوصف: | The crystal structure of a conserved domain of nonstructural protein 3 (nsP3) from severe acute respiratory syndrome coronavirus (SARS-CoV) has been solved by single-wavelength anomalous dispersion to 1.4 A resolution. The structure of this "X" domain, seen in many single-stranded RNA viruses, reveals a three-layered alpha/beta/alpha core with a macro-H2A-like fold. The putative active site is a solvent-exposed cleft that is conserved in its three structural homologs, yeast Ymx7, Archeoglobus fulgidus AF1521, and Er58 from E. coli. Its sequence is similar to yeast YBR022W (also known as Poa1P), a known phosphatase that acts on ADP-ribose-1''-phosphate (Appr-1''-p). The SARS nsP3 domain readily removes the 1'' phosphate group from Appr-1''-p in in vitro assays, confirming its phosphatase activity. Sequence and structure comparison of all known macro-H2A domains combined with available functional data suggests that proteins of this superfamily form an emerging group of nucleotide phosphatases that dephosphorylate Appr-1''-p. |
| وصف الملف: | application/pdf |
| تدمد: | 0969-2126 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::347a106b53be991a8187dd1be5d4c49e https://pubmed.ncbi.nlm.nih.gov/16271880 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....347a106b53be991a8187dd1be5d4c49e |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 09692126 |
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