Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs
Identifieur interne : 004695 ( Main/Merge ); précédent : 004694; suivant : 004696Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs
Auteurs : Jeremiah S. Joseph [États-Unis] ; KUMAR SINGH SAIKATENDU [États-Unis] ; Vanitha Subramanian [États-Unis] ; Benjamin W. Neuman [États-Unis] ; Alexei Brooun [États-Unis] ; Mark Griffith [États-Unis] ; Kin Moy [États-Unis] ; Maneesh K. Yadav [États-Unis] ; Jeffrey Velasquez [États-Unis] ; Michael J. Buchmeier [États-Unis] ; Raymond C. Stevens [États-Unis] ; Peter Kuhn [États-Unis]Source :
- Journal of virology [ 0022-538X ] ; 2006.
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English descriptors
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Abstract
The severe acute respiratory syndrome coronavirus (SARS-CoV) possesses a large 29.7-kb positive-stranded RNA genome. The first open reading frame encodes replicase polyproteins la and lab, which are cleaved to generate 16 "nonstructural" proteins, nspl to nspl6, involved in viral replication and/or RNA processing. Among these, nsp10 plays a critical role in minus-strand RNA synthesis in a related coronavirus, murine hepatitis virus. Here, we report the crystal structure of SARS-CoV nsp10 at a resolution of 1.8 Å as determined by single-wavelength anomalous dispersion using phases derived from hexatantalum dodecabromide. nsp10 is a single domain protein consisting of a pair of antiparallel N-terminal helices stacked against an irregular β-sheet, a coil-rich C terminus, and two Zn fingers. nsp10 represents a novel fold and is the first structural representative of this family of Zn finger proteins found so far exclusively in coronaviruses. The first Zn finger coordinates a Zn2+ ion in a unique conformation. The second Zn finger, with four cysteines, is a distant member of the "gag-knuckle fold group" of Zn2+-binding domains and appears to maintain the structural integrity of the C-terminal tail. A distinct clustering of basic residues on the protein surface suggests a nucleic acid-binding function. Gel shift assays indicate that in isolation, nsp10 binds single- and double-stranded RNA and DNA with high-micromolar affinity and without obvious sequence specificity. It is possible that nsp10 functions within a larger RNA-binding protein complex. However, its exact role within the replicase complex is still not clear.
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs</title>
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<country>États-Unis</country>
<wicri:noRegion>La Jolla, California 92037</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Stevens, Raymond C" sort="Stevens, Raymond C" uniqKey="Stevens R" first="Raymond C." last="Stevens">Raymond C. Stevens</name>
<affiliation wicri:level="1"><inist:fA14 i1="02"><s1>Department of Molecular Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road</s1>
<s2>La Jolla, California 92037</s2>
<s3>USA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>11 aut.</sZ>
</inist:fA14>
<country>États-Unis</country>
<wicri:noRegion>La Jolla, California 92037</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Kuhn, Peter" sort="Kuhn, Peter" uniqKey="Kuhn P" first="Peter" last="Kuhn">Peter Kuhn</name>
<affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road</s1>
<s2>La Jolla, California 92037</s2>
<s3>USA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>12 aut.</sZ>
</inist:fA14>
<country>États-Unis</country>
<wicri:noRegion>La Jolla, California 92037</wicri:noRegion>
</affiliation>
</author>
</analytic>
<series><title level="j" type="main">Journal of virology</title>
<title level="j" type="abbreviated">J. virol.</title>
<idno type="ISSN">0022-538X</idno>
<imprint><date when="2006">2006</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
<seriesStmt><title level="j" type="main">Journal of virology</title>
<title level="j" type="abbreviated">J. virol.</title>
<idno type="ISSN">0022-538X</idno>
</seriesStmt>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Coronavirus</term>
<term>Crystalline structure</term>
<term>Microbiology</term>
<term>Protein</term>
<term>Severe acute respiratory syndrome</term>
<term>Virology</term>
</keywords>
<keywords scheme="Pascal" xml:lang="fr"><term>Coronavirus</term>
<term>Structure cristalline</term>
<term>Protéine</term>
<term>Microbiologie</term>
<term>Virologie</term>
<term>Syndrome respiratoire aigu sévère</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">The severe acute respiratory syndrome coronavirus (SARS-CoV) possesses a large 29.7-kb positive-stranded RNA genome. The first open reading frame encodes replicase polyproteins la and lab, which are cleaved to generate 16 "nonstructural" proteins, nspl to nspl6, involved in viral replication and/or RNA processing. Among these, nsp10 plays a critical role in minus-strand RNA synthesis in a related coronavirus, murine hepatitis virus. Here, we report the crystal structure of SARS-CoV nsp10 at a resolution of 1.8 Å as determined by single-wavelength anomalous dispersion using phases derived from hexatantalum dodecabromide. nsp10 is a single domain protein consisting of a pair of antiparallel N-terminal helices stacked against an irregular β-sheet, a coil-rich C terminus, and two Zn fingers. nsp10 represents a novel fold and is the first structural representative of this family of Zn finger proteins found so far exclusively in coronaviruses. The first Zn finger coordinates a Zn<sup>2+</sup>
ion in a unique conformation. The second Zn finger, with four cysteines, is a distant member of the "gag-knuckle fold group" of Zn<sup>2+</sup>
-binding domains and appears to maintain the structural integrity of the C-terminal tail. A distinct clustering of basic residues on the protein surface suggests a nucleic acid-binding function. Gel shift assays indicate that in isolation, nsp10 binds single- and double-stranded RNA and DNA with high-micromolar affinity and without obvious sequence specificity. It is possible that nsp10 functions within a larger RNA-binding protein complex. However, its exact role within the replicase complex is still not clear.</div>
</front>
</TEI>
<affiliations><list><country><li>États-Unis</li>
</country>
</list>
<tree><country name="États-Unis"><noRegion><name sortKey="Joseph, Jeremiah S" sort="Joseph, Jeremiah S" uniqKey="Joseph J" first="Jeremiah S." last="Joseph">Jeremiah S. Joseph</name>
</noRegion>
<name sortKey="Brooun, Alexei" sort="Brooun, Alexei" uniqKey="Brooun A" first="Alexei" last="Brooun">Alexei Brooun</name>
<name sortKey="Buchmeier, Michael J" sort="Buchmeier, Michael J" uniqKey="Buchmeier M" first="Michael J." last="Buchmeier">Michael J. Buchmeier</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="Kumar Singh Saikatendu" sort="Kumar Singh Saikatendu" uniqKey="Kumar Singh Saikatendu" last="Kumar Singh Saikatendu">KUMAR SINGH SAIKATENDU</name>
<name sortKey="Kumar Singh Saikatendu" sort="Kumar Singh Saikatendu" uniqKey="Kumar Singh Saikatendu" last="Kumar Singh Saikatendu">KUMAR SINGH SAIKATENDU</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="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="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>
<name sortKey="Yadav, Maneesh K" sort="Yadav, Maneesh K" uniqKey="Yadav M" first="Maneesh K." last="Yadav">Maneesh K. Yadav</name>
</country>
</tree>
</affiliations>
</record>
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