Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs
Identifieur interne : 004465 ( Main/Exploration ); précédent : 004464; suivant : 004466Crystal 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.
Descripteurs français
- KwdFr :
- MESH :
- physiologie : Protéines virales non structurales.
- Pascal (Inist)
- Conformation des protéines, Coronavirus, Cristallographie aux rayons X, Doigts de zinc, Données de séquences moléculaires, Pliage des protéines, Protéines virales non structurales, Structure cristalline, Protéine, Microbiologie, Séquence d'acides aminés, Virologie, Syndrome respiratoire aigu sévère, Virus du SRAS.
English descriptors
- KwdEn :
- Amino Acid Sequence, Coronavirus, Crystalline structure, Crystallography, X-Ray, Microbiology, Molecular Sequence Data, Protein, Protein Conformation, Protein Folding, SARS Virus, Severe acute respiratory syndrome, Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (physiology), Virology, Zinc Fingers.
- MESH :
- chemical , chemistry : Viral Nonstructural Proteins.
- chemical , physiology : Viral Nonstructural Proteins.
- Amino Acid Sequence, Crystallography, X-Ray, Molecular Sequence Data, Protein Conformation, Protein Folding, SARS Virus, Zinc Fingers.
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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Joseph</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><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="Kumar Singh Saikatendu" sort="Kumar Singh Saikatendu" uniqKey="Kumar Singh Saikatendu" last="Kumar Singh Saikatendu">KUMAR SINGH SAIKATENDU</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><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="Subramanian, Vanitha" sort="Subramanian, Vanitha" uniqKey="Subramanian V" first="Vanitha" last="Subramanian">Vanitha Subramanian</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><affiliation wicri:level="1"><inist:fA14 i1="02"><s1>Department of Molecular Biology, The Scripps Research Institute, 10550 N. 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Torrey Pines Road</s1><s2>La Jolla, California 92037</s2><s3>USA</s3><sZ>4 aut.</sZ><sZ>10 aut.</sZ></inist:fA14><country>États-Unis</country><wicri:noRegion>La Jolla, California 92037</wicri:noRegion></affiliation></author><author><name sortKey="Brooun, Alexei" sort="Brooun, Alexei" uniqKey="Brooun A" first="Alexei" last="Brooun">Alexei Brooun</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><author><name sortKey="Griffith, Mark" sort="Griffith, Mark" uniqKey="Griffith M" first="Mark" last="Griffith">Mark Griffith</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="Moy, Kin" sort="Moy, Kin" uniqKey="Moy K" first="Kin" last="Moy">Kin Moy</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="Yadav, Maneesh K" sort="Yadav, Maneesh K" uniqKey="Yadav M" first="Maneesh K." last="Yadav">Maneesh K. Yadav</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><author><name sortKey="Velasquez, Jeffrey" sort="Velasquez, Jeffrey" uniqKey="Velasquez J" first="Jeffrey" last="Velasquez">Jeffrey Velasquez</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="Buchmeier, Michael J" sort="Buchmeier, Michael J" uniqKey="Buchmeier M" first="Michael J." last="Buchmeier">Michael J. Buchmeier</name><affiliation wicri:level="1"><inist: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><sZ>10 aut.</sZ></inist:fA14><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>Amino Acid Sequence</term><term>Coronavirus</term><term>Crystalline structure</term><term>Crystallography, X-Ray</term><term>Microbiology</term><term>Molecular Sequence Data</term><term>Protein</term><term>Protein Conformation</term><term>Protein Folding</term><term>SARS Virus</term><term>Severe acute respiratory syndrome</term><term>Viral Nonstructural Proteins (chemistry)</term><term>Viral Nonstructural Proteins (physiology)</term><term>Virology</term><term>Zinc Fingers</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Doigts de zinc</term><term>Données de séquences moléculaires</term><term>Pliage des protéines</term><term>Protéines virales non structurales ()</term><term>Protéines virales non structurales (physiologie)</term><term>Séquence d'acides aminés</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Protéines virales non structurales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Crystallography, X-Ray</term><term>Molecular Sequence Data</term><term>Protein Conformation</term><term>Protein Folding</term><term>SARS Virus</term><term>Zinc Fingers</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Conformation des protéines</term><term>Coronavirus</term><term>Cristallographie aux rayons X</term><term>Doigts de zinc</term><term>Données de séquences moléculaires</term><term>Pliage des protéines</term><term>Protéines virales non structurales</term><term>Structure cristalline</term><term>Protéine</term><term>Microbiologie</term><term>Séquence d'acides aminés</term><term>Virologie</term><term>Syndrome respiratoire aigu sévère</term><term>Virus du SRAS</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>Pour manipuler ce document sous Unix (Dilib)
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