Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs
Identifieur interne : 000494 ( PascalFrancis/Checkpoint ); précédent : 000493; suivant : 000495Crystal 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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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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<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>
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<country>États-Unis</country>
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<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>
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<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>
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<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>
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<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>
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<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>
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<inist><standard h6="B"><pA><fA01 i1="01" i2="1"><s0>0022-538X</s0>
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<fA03 i2="1"><s0>J. virol.</s0>
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<fA05><s2>80</s2>
</fA05>
<fA06><s2>16</s2>
</fA06>
<fA08 i1="01" i2="1" l="ENG"><s1>Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs</s1>
</fA08>
<fA11 i1="01" i2="1"><s1>JOSEPH (Jeremiah S.)</s1>
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<fA11 i1="02" i2="1"><s1>KUMAR SINGH SAIKATENDU</s1>
</fA11>
<fA11 i1="03" i2="1"><s1>SUBRAMANIAN (Vanitha)</s1>
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<fA11 i1="04" i2="1"><s1>NEUMAN (Benjamin W.)</s1>
</fA11>
<fA11 i1="05" i2="1"><s1>BROOUN (Alexei)</s1>
</fA11>
<fA11 i1="06" i2="1"><s1>GRIFFITH (Mark)</s1>
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<fA11 i1="07" i2="1"><s1>MOY (Kin)</s1>
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<fA11 i1="08" i2="1"><s1>YADAV (Maneesh K.)</s1>
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<fA11 i1="09" i2="1"><s1>VELASQUEZ (Jeffrey)</s1>
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<fA11 i1="10" i2="1"><s1>BUCHMEIER (Michael J.)</s1>
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<fA11 i1="11" i2="1"><s1>STEVENS (Raymond C.)</s1>
</fA11>
<fA11 i1="12" i2="1"><s1>KUHN (Peter)</s1>
</fA11>
<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>
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<sZ>2 aut.</sZ>
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<sZ>8 aut.</sZ>
<sZ>12 aut.</sZ>
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<fA14 i1="02"><s1>Department of Molecular Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road</s1>
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<s3>USA</s3>
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<fA14 i1="03"><s1>Department of Neumpharmacolagy, The Scripps Research Institute, 10550 N. Torrey Pines Road</s1>
<s2>La Jolla, California 92037</s2>
<s3>USA</s3>
<sZ>4 aut.</sZ>
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<fC01 i1="01" l="ENG"><s0>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.</s0>
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<s2>NW</s2>
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<s2>NW</s2>
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<s2>NW</s2>
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<s2>NW</s2>
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<s2>NW</s2>
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<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>
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<name sortKey="Moy, Kin" sort="Moy, Kin" uniqKey="Moy K" first="Kin" last="Moy">Kin Moy</name>
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<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>
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