Structural Genomics of the Severe Acute Respiratory Syndrome Coronavirus: Nuclear Magnetic Resonance Structure of the Protein nsP7
Identifieur interne : 000699 ( Pmc/Corpus ); précédent : 000698; suivant : 000700Structural Genomics of the Severe Acute Respiratory Syndrome Coronavirus: Nuclear Magnetic Resonance Structure of the Protein nsP7
Auteurs : Wolfgang Peti ; Margaret A. Johnson ; Torsten Herrmann ; Benjamin W. Neuman ; Michael J. Buchmeier ; Mike Nelson ; Jeremiah Joseph ; Rebecca Page ; Raymond C. Stevens ; Peter Kuhn ; Kurt WüthrichSource :
- Journal of Virology [ 0022-538X ] ; 2005.
Abstract
Here, we report the three-dimensional structure of severe acute respiratory syndrome coronavirus (SARS-CoV) nsP7, a component of the SARS-CoV replicase polyprotein. The coronavirus replicase carries out regulatory tasks involved in the maintenance, transcription, and replication of the coronavirus genome. nsP7 was found to assume a compact architecture in solution, which is comprised primarily of helical secondary structures. Three helices (α2 to α4) form a flat up-down-up antiparallel α-helix sheet. The N-terminal segment of residues 1 to 22, containing two turns of α-helix and one turn of 310-helix, is packed across the surface of α2 and α3 in the helix sheet, with the α-helical region oriented at a 60° angle relative to α2 and α3. The surface charge distribution is pronouncedly asymmetrical, with the flat surface of the helical sheet showing a large negatively charged region adjacent to a large hydrophobic patch and the opposite side containing a positively charged groove that extends along the helix α1. Each of these three areas is thus implicated as a potential site for protein-protein interactions.
Url:
DOI: 10.1128/JVI.79.20.12905-12913.2005
PubMed: 16188992
PubMed Central: 1235862
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The coronavirus replicase carries out regulatory tasks involved in the maintenance, transcription, and replication of the coronavirus genome. nsP7 was found to assume a compact architecture in solution, which is comprised primarily of helical secondary structures. Three helices (α2 to α4) form a flat up-down-up antiparallel α-helix sheet. The N-terminal segment of residues 1 to 22, containing two turns of α-helix and one turn of 3<sub>10</sub>-helix, is packed across the surface of α2 and α3 in the helix sheet, with the α-helical region oriented at a 60° angle relative to α2 and α3. The surface charge distribution is pronouncedly asymmetrical, with the flat surface of the helical sheet showing a large negatively charged region adjacent to a large hydrophobic patch and the opposite side containing a positively charged groove that extends along the helix α1. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">J Virol</journal-id><journal-id journal-id-type="publisher-id">jvi</journal-id><journal-title>Journal of Virology</journal-title><issn pub-type="ppub">0022-538X</issn><issn pub-type="epub">1098-5514</issn><publisher><publisher-name>American Society for Microbiology</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">16188992</article-id><article-id pub-id-type="pmc">1235862</article-id><article-id pub-id-type="publisher-id">1191-05</article-id><article-id pub-id-type="doi">10.1128/JVI.79.20.12905-12913.2005</article-id><article-categories><subj-group subj-group-type="heading"><subject>Structure and Assembly</subject></subj-group></article-categories><title-group><article-title>Structural Genomics of the Severe Acute Respiratory Syndrome Coronavirus: Nuclear Magnetic Resonance Structure of the Protein nsP7</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Peti</surname><given-names>Wolfgang</given-names></name><xref ref-type="aff" rid="aff1">1</xref><xref ref-type="aff" rid="aff1">2</xref><xref ref-type="fn" rid="fn1">†</xref></contrib><contrib contrib-type="author"><name><surname>Johnson</surname><given-names>Margaret A.</given-names></name><xref ref-type="aff" rid="aff1">1</xref><xref ref-type="aff" rid="aff1">2</xref></contrib><contrib contrib-type="author"><name><surname>Herrmann</surname><given-names>Torsten</given-names></name><xref ref-type="aff" rid="aff1">1</xref><xref ref-type="fn" rid="fn2">‡</xref></contrib><contrib contrib-type="author"><name><surname>Neuman</surname><given-names>Benjamin W.</given-names></name><xref ref-type="aff" rid="aff1">2</xref><xref ref-type="aff" rid="aff1">3</xref></contrib><contrib contrib-type="author"><name><surname>Buchmeier</surname><given-names>Michael J.</given-names></name><xref ref-type="aff" rid="aff1">2</xref><xref ref-type="aff" rid="aff1">3</xref></contrib><contrib contrib-type="author"><name><surname>Nelson</surname><given-names>Mike</given-names></name><xref ref-type="aff" rid="aff1">1</xref><xref ref-type="aff" rid="aff1">2</xref></contrib><contrib contrib-type="author"><name><surname>Joseph</surname><given-names>Jeremiah</given-names></name><xref ref-type="aff" rid="aff1">2</xref><xref ref-type="aff" rid="aff1">4</xref></contrib><contrib contrib-type="author"><name><surname>Page</surname><given-names>Rebecca</given-names></name><xref ref-type="aff" rid="aff1">1</xref><xref ref-type="aff" rid="aff1">5</xref><xref ref-type="fn" rid="fn3">§</xref></contrib><contrib contrib-type="author"><name><surname>Stevens</surname><given-names>Raymond C.</given-names></name><xref ref-type="aff" rid="aff1">1</xref><xref ref-type="aff" rid="aff1">2</xref><xref ref-type="aff" rid="aff1">5</xref></contrib><contrib contrib-type="author"><name><surname>Kuhn</surname><given-names>Peter</given-names></name><xref ref-type="aff" rid="aff1">2</xref><xref ref-type="aff" rid="aff1">4</xref><xref ref-type="aff" rid="aff1">5</xref><xref ref-type="corresp" rid="cor1">*</xref></contrib><contrib contrib-type="author"><name><surname>Wüthrich</surname><given-names>Kurt</given-names></name><xref ref-type="aff" rid="aff1">1</xref><xref ref-type="aff" rid="aff1">2</xref><xref ref-type="aff" rid="aff1">5</xref><xref ref-type="corresp" rid="cor1">*</xref></contrib></contrib-group><aff id="aff1">Department of Molecular Biology,<label>1</label> Consortium for Functional and Structural Proteomics of SARS-CoV Related Proteins,<label>2</label> Department of Neuropharmacology,<label>3</label> Department of Cell Biology,<label>4</label> Joint Center for Structural Genomics, The Scripps Research Institute, 10550 North Torrey Pines Rd., La Jolla, California 92037<label>5</label></aff><author-notes><fn id="cor1"><label>*</label><p>Corresponding author. Mailing address for Peter Kuhn: Department of Cell Biology, The Scripps Research Institute, 10550 North Torrey Pines Rd., CB-265, La Jolla, CA 92037. Phone: (858) 784-9114. Fax: (858) 784-8996. E-mail: <email>pkuhn@scripps.edu</email>. Mailing address for Kurt Wüthrich: Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Rd., MB-44, La Jolla, CA 92037. Phone: (858) 784-8011. Fax: (858) 784-8014. E-mail: <email>wuthrich@scripps.edu</email>.</p></fn><fn id="fn1"><label>†</label><p>Present address: Brown University, Department of Molecular Pharmacology, Physiology and Biotechnology, 70 Ship Street, GE-3, Providence, RI 02912.</p></fn><fn id="fn2"><label>‡</label><p>Present address: Institut für Molekularbiologie und Biophysik, ETH Zürich, CH-8093 Zürich, Switzerland.</p></fn><fn id="fn3"><label>§</label><p>Present address: Brown University, Department of Molecular Biology, Cell Biology and Biochemistry, 70 Ship Street, GE-4, Providence, RI 02912.</p></fn></author-notes><pub-date pub-type="ppub"><month>10</month><year>2005</year></pub-date><volume>79</volume><issue>20</issue><fpage>12905</fpage><lpage>12913</lpage><history><date date-type="received"><day>9</day><month>6</month><year>2005</year></date><date date-type="accepted"><day>22</day><month>7</month><year>2005</year></date></history><copyright-statement>Copyright © 2005, American Society for Microbiology</copyright-statement><copyright-year>2005</copyright-year><abstract><p>Here, we report the three-dimensional structure of severe acute respiratory syndrome coronavirus (SARS-CoV) nsP7, a component of the SARS-CoV replicase polyprotein. The coronavirus replicase carries out regulatory tasks involved in the maintenance, transcription, and replication of the coronavirus genome. nsP7 was found to assume a compact architecture in solution, which is comprised primarily of helical secondary structures. Three helices (α2 to α4) form a flat up-down-up antiparallel α-helix sheet. The N-terminal segment of residues 1 to 22, containing two turns of α-helix and one turn of 3<sub>10</sub>-helix, is packed across the surface of α2 and α3 in the helix sheet, with the α-helical region oriented at a 60° angle relative to α2 and α3. The surface charge distribution is pronouncedly asymmetrical, with the flat surface of the helical sheet showing a large negatively charged region adjacent to a large hydrophobic patch and the opposite side containing a positively charged groove that extends along the helix α1. Each of these three areas is thus implicated as a potential site for protein-protein interactions.</p></abstract><custom-meta-wrap><custom-meta><meta-name>PDF filename</meta-name><meta-value>zjv02005012905</meta-value></custom-meta></custom-meta-wrap></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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