Structural Basis of Severe Acute Respiratory Syndrome Coronavirus ADP-Ribose-1″-Phosphate Dephosphorylation by a Conserved Domain of nsP3
Identifieur interne : 001223 ( Pmc/Checkpoint ); précédent : 001222; suivant : 001224Structural Basis of Severe Acute Respiratory Syndrome Coronavirus ADP-Ribose-1″-Phosphate Dephosphorylation by a Conserved Domain of nsP3
Auteurs : Kumar Singh Saikatendu ; Jeremiah S. Joseph ; Vanitha Subramanian ; Tom Clayton ; Mark Griffith ; Kin Moy ; Jeffrey Velasquez ; Benjamin W. Neuman ; Michael J. Buchmeier ; Raymond C. Stevens ; Peter KuhnSource :
- Structure (London, England : 1993) [ 0969-2126 ] ; 2005.
Abstract
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 Å resolution. The structure of this “X” domain, seen in many single-stranded RNA viruses, reveals a three-layered α/β/α 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,
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DOI: 10.1016/j.str.2005.07.022
PubMed: 16271890
PubMed Central: 7126892
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Structural Basis of Severe Acute Respiratory Syndrome Coronavirus ADP-Ribose-1″-Phosphate Dephosphorylation by a Conserved Domain of nsP3</title><author><name sortKey="Saikatendu, Kumar Singh" sort="Saikatendu, Kumar Singh" uniqKey="Saikatendu K" first="Kumar Singh" last="Saikatendu">Kumar Singh Saikatendu</name></author><author><name sortKey="Joseph, Jeremiah S" sort="Joseph, Jeremiah S" uniqKey="Joseph J" first="Jeremiah S." last="Joseph">Jeremiah S. Joseph</name></author><author><name sortKey="Subramanian, Vanitha" sort="Subramanian, Vanitha" uniqKey="Subramanian V" first="Vanitha" last="Subramanian">Vanitha Subramanian</name></author><author><name sortKey="Clayton, Tom" sort="Clayton, Tom" uniqKey="Clayton T" first="Tom" last="Clayton">Tom Clayton</name></author><author><name sortKey="Griffith, Mark" sort="Griffith, Mark" uniqKey="Griffith M" first="Mark" last="Griffith">Mark Griffith</name></author><author><name sortKey="Moy, Kin" sort="Moy, Kin" uniqKey="Moy K" first="Kin" last="Moy">Kin Moy</name></author><author><name sortKey="Velasquez, Jeffrey" sort="Velasquez, Jeffrey" uniqKey="Velasquez J" first="Jeffrey" last="Velasquez">Jeffrey Velasquez</name></author><author><name sortKey="Neuman, Benjamin W" sort="Neuman, Benjamin W" uniqKey="Neuman B" first="Benjamin W." last="Neuman">Benjamin W. Neuman</name></author><author><name sortKey="Buchmeier, Michael J" sort="Buchmeier, Michael J" uniqKey="Buchmeier M" first="Michael J." last="Buchmeier">Michael J. Buchmeier</name></author><author><name sortKey="Stevens, Raymond C" sort="Stevens, Raymond C" uniqKey="Stevens R" first="Raymond C." last="Stevens">Raymond C. Stevens</name></author><author><name sortKey="Kuhn, Peter" sort="Kuhn, Peter" uniqKey="Kuhn P" first="Peter" last="Kuhn">Peter Kuhn</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">16271890</idno><idno type="pmc">7126892</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7126892</idno><idno type="RBID">PMC:7126892</idno><idno type="doi">10.1016/j.str.2005.07.022</idno><date when="2005">2005</date><idno type="wicri:Area/Pmc/Corpus">001491</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">001491</idno><idno type="wicri:Area/Pmc/Curation">001491</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">001491</idno><idno type="wicri:Area/Pmc/Checkpoint">001223</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">001223</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Structural Basis of Severe Acute Respiratory Syndrome Coronavirus ADP-Ribose-1″-Phosphate Dephosphorylation by a Conserved Domain of nsP3</title><author><name sortKey="Saikatendu, Kumar Singh" sort="Saikatendu, Kumar Singh" uniqKey="Saikatendu K" first="Kumar Singh" last="Saikatendu">Kumar Singh Saikatendu</name></author><author><name sortKey="Joseph, Jeremiah S" sort="Joseph, Jeremiah S" uniqKey="Joseph J" first="Jeremiah S." last="Joseph">Jeremiah S. Joseph</name></author><author><name sortKey="Subramanian, Vanitha" sort="Subramanian, Vanitha" uniqKey="Subramanian V" first="Vanitha" last="Subramanian">Vanitha Subramanian</name></author><author><name sortKey="Clayton, Tom" sort="Clayton, Tom" uniqKey="Clayton T" first="Tom" last="Clayton">Tom Clayton</name></author><author><name sortKey="Griffith, Mark" sort="Griffith, Mark" uniqKey="Griffith M" first="Mark" last="Griffith">Mark Griffith</name></author><author><name sortKey="Moy, Kin" sort="Moy, Kin" uniqKey="Moy K" first="Kin" last="Moy">Kin Moy</name></author><author><name sortKey="Velasquez, Jeffrey" sort="Velasquez, Jeffrey" uniqKey="Velasquez J" first="Jeffrey" last="Velasquez">Jeffrey Velasquez</name></author><author><name sortKey="Neuman, Benjamin W" sort="Neuman, Benjamin W" uniqKey="Neuman B" first="Benjamin W." last="Neuman">Benjamin W. Neuman</name></author><author><name sortKey="Buchmeier, Michael J" sort="Buchmeier, Michael J" uniqKey="Buchmeier M" first="Michael J." last="Buchmeier">Michael J. Buchmeier</name></author><author><name sortKey="Stevens, Raymond C" sort="Stevens, Raymond C" uniqKey="Stevens R" first="Raymond C." last="Stevens">Raymond C. Stevens</name></author><author><name sortKey="Kuhn, Peter" sort="Kuhn, Peter" uniqKey="Kuhn P" first="Peter" last="Kuhn">Peter Kuhn</name></author></analytic><series><title level="j">Structure (London, England : 1993)</title><idno type="ISSN">0969-2126</idno><idno type="eISSN">1878-4186</idno><imprint><date when="2005">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>Summary</title><p>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 Å resolution. The structure of this “X” domain, seen in many single-stranded RNA viruses, reveals a three-layered α/β/α 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, <italic>Archeoglobus fulgidus</italic> AF1521, and Er58 from <italic>E. coli</italic>. 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.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Allen, M D" uniqKey="Allen M">M.D. Allen</name></author><author><name sortKey="Buckle, A M" uniqKey="Buckle A">A.M. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Structure</journal-id><journal-id journal-id-type="iso-abbrev">Structure</journal-id><journal-title-group><journal-title>Structure (London, England : 1993)</journal-title></journal-title-group><issn pub-type="ppub">0969-2126</issn><issn pub-type="epub">1878-4186</issn><publisher><publisher-name>Elsevier Ltd.</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">16271890</article-id><article-id pub-id-type="pmc">7126892</article-id><article-id pub-id-type="publisher-id">S0969-2126(05)00313-8</article-id><article-id pub-id-type="doi">10.1016/j.str.2005.07.022</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Structural Basis of Severe Acute Respiratory Syndrome Coronavirus ADP-Ribose-1″-Phosphate Dephosphorylation by a Conserved Domain of nsP3</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Saikatendu</surname><given-names>Kumar Singh</given-names></name><xref rid="fn1" ref-type="fn">1</xref></contrib><contrib contrib-type="author"><name><surname>Joseph</surname><given-names>Jeremiah S.</given-names></name><xref rid="fn1" ref-type="fn">1</xref></contrib><contrib contrib-type="author"><name><surname>Subramanian</surname><given-names>Vanitha</given-names></name></contrib><contrib contrib-type="author"><name><surname>Clayton</surname><given-names>Tom</given-names></name></contrib><contrib contrib-type="author"><name><surname>Griffith</surname><given-names>Mark</given-names></name></contrib><contrib contrib-type="author"><name><surname>Moy</surname><given-names>Kin</given-names></name></contrib><contrib contrib-type="author"><name><surname>Velasquez</surname><given-names>Jeffrey</given-names></name></contrib><contrib contrib-type="author"><name><surname>Neuman</surname><given-names>Benjamin W.</given-names></name></contrib><contrib contrib-type="author"><name><surname>Buchmeier</surname><given-names>Michael J.</given-names></name></contrib><contrib contrib-type="author"><name><surname>Stevens</surname><given-names>Raymond C.</given-names></name></contrib><contrib contrib-type="author"><name><surname>Kuhn</surname><given-names>Peter</given-names></name><email>pkuhn@scripps.edu</email><xref rid="cor1" ref-type="corresp">∗</xref></contrib></contrib-group><aff>Departments of Cell Biology, Molecular Biology, and Neuropharmacology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037</aff><author-notes><corresp id="cor1"><label>∗</label>Ph: 858-784-9114; Fax: 858-784-8996 <email>pkuhn@scripps.edu</email></corresp><fn id="fn1"><label>1</label><p>These authors contributed equally to this work.</p></fn></author-notes><pub-date pub-type="pmc-release"><day>8</day><month>11</month><year>2005</year></pub-date><pmc-comment> PMC Release delay is 0 months and 0 days and was based on .</pmc-comment>
<pub-date pub-type="ppub"><month>11</month><year>2005</year></pub-date><pub-date pub-type="epub"><day>8</day><month>11</month><year>2005</year></pub-date><volume>13</volume><issue>11</issue><fpage>1665</fpage><lpage>1675</lpage><history><date date-type="received"><day>27</day><month>5</month><year>2005</year></date><date date-type="rev-recd"><day>26</day><month>7</month><year>2005</year></date><date date-type="accepted"><day>31</day><month>7</month><year>2005</year></date></history><permissions><copyright-statement>Copyright © 2005 Elsevier Ltd. All rights reserved.</copyright-statement><copyright-year>2005</copyright-year><copyright-holder>Elsevier Ltd</copyright-holder><license><license-p>Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.</license-p></license></permissions><abstract><title>Summary</title><p>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 Å resolution. The structure of this “X” domain, seen in many single-stranded RNA viruses, reveals a three-layered α/β/α 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, <italic>Archeoglobus fulgidus</italic> AF1521, and Er58 from <italic>E. coli</italic>. 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.</p></abstract></article-meta><notes><p>Published: November 8, 2005</p></notes></front></pmc><affiliations><list></list><tree><noCountry><name sortKey="Buchmeier, Michael J" sort="Buchmeier, Michael J" uniqKey="Buchmeier M" first="Michael J." last="Buchmeier">Michael J. Buchmeier</name><name sortKey="Clayton, Tom" sort="Clayton, Tom" uniqKey="Clayton T" first="Tom" last="Clayton">Tom Clayton</name><name sortKey="Griffith, Mark" sort="Griffith, Mark" uniqKey="Griffith M" first="Mark" last="Griffith">Mark Griffith</name><name sortKey="Joseph, Jeremiah S" sort="Joseph, Jeremiah S" uniqKey="Joseph J" first="Jeremiah S." last="Joseph">Jeremiah S. Joseph</name><name sortKey="Kuhn, Peter" sort="Kuhn, Peter" uniqKey="Kuhn P" first="Peter" last="Kuhn">Peter Kuhn</name><name sortKey="Moy, Kin" sort="Moy, Kin" uniqKey="Moy K" first="Kin" last="Moy">Kin Moy</name><name sortKey="Neuman, Benjamin W" sort="Neuman, Benjamin W" uniqKey="Neuman B" first="Benjamin W." last="Neuman">Benjamin W. Neuman</name><name sortKey="Saikatendu, Kumar Singh" sort="Saikatendu, Kumar Singh" uniqKey="Saikatendu K" first="Kumar Singh" last="Saikatendu">Kumar Singh Saikatendu</name><name sortKey="Stevens, Raymond C" sort="Stevens, Raymond C" uniqKey="Stevens R" first="Raymond C." last="Stevens">Raymond C. Stevens</name><name sortKey="Subramanian, Vanitha" sort="Subramanian, Vanitha" uniqKey="Subramanian V" first="Vanitha" last="Subramanian">Vanitha Subramanian</name><name sortKey="Velasquez, Jeffrey" sort="Velasquez, Jeffrey" uniqKey="Velasquez J" first="Jeffrey" last="Velasquez">Jeffrey Velasquez</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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HfdIndexSelect -h $EXPLOR_AREA/Data/Pmc/Checkpoint/RBID.i -Sk "pubmed:16271890" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Pmc/Checkpoint/biblio.hfd \
| NlmPubMed2Wicri -a SrasV1
| This area was generated with Dilib version V0.6.33. |  |