Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs.
Identifieur interne : 002240 ( PubMed/Checkpoint ); précédent : 002239; suivant : 002241Crystal 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 ; Vanitha Subramanian ; Benjamin W. Neuman ; Alexei Brooun ; Mark Griffith ; Kin Moy ; Maneesh K. Yadav ; Jeffrey Velasquez ; Michael J. Buchmeier ; Raymond C. Stevens ; Peter KuhnSource :
- Journal of virology [ 0022-538X ] ; 2006.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- 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 1a and 1ab, which are cleaved to generate 16 "nonstructural" proteins, nsp1 to nsp16, 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 A 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 beta-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.
DOI: 10.1128/JVI.00467-06
PubMed: 16873246
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Joseph</name><affiliation wicri:level="1"><nlm:affiliation>Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, California 92037, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, California 92037</wicri:regionArea><wicri:noRegion>California 92037</wicri:noRegion></affiliation></author><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="Subramanian, Vanitha" sort="Subramanian, Vanitha" uniqKey="Subramanian V" first="Vanitha" last="Subramanian">Vanitha Subramanian</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="Brooun, Alexei" sort="Brooun, Alexei" uniqKey="Brooun A" first="Alexei" last="Brooun">Alexei Brooun</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="Yadav, Maneesh K" sort="Yadav, Maneesh K" uniqKey="Yadav M" first="Maneesh K" last="Yadav">Maneesh K. Yadav</name></author><author><name sortKey="Velasquez, Jeffrey" sort="Velasquez, Jeffrey" uniqKey="Velasquez J" first="Jeffrey" last="Velasquez">Jeffrey Velasquez</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">Journal of virology</title><idno type="ISSN">0022-538X</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" 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>Viral Nonstructural Proteins (chemistry)</term><term>Viral Nonstructural Proteins (physiology)</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="MESH" 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>Séquence d'acides aminés</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 1a and 1ab, which are cleaved to generate 16 "nonstructural" proteins, nsp1 to nsp16, 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 A 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 beta-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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16873246</PMID><DateCompleted><Year>2006</Year><Month>09</Month><Day>14</Day></DateCompleted><DateRevised><Year>2018</Year><Month>12</Month><Day>27</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0022-538X</ISSN><JournalIssue CitedMedium="Print"><Volume>80</Volume><Issue>16</Issue><PubDate><Year>2006</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Journal of virology</Title><ISOAbbreviation>J. Virol.</ISOAbbreviation></Journal><ArticleTitle>Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs.</ArticleTitle><Pagination><MedlinePgn>7894-901</MedlinePgn></Pagination><Abstract><AbstractText>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 1a and 1ab, which are cleaved to generate 16 "nonstructural" proteins, nsp1 to nsp16, 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 A 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 beta-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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Joseph</LastName><ForeName>Jeremiah S</ForeName><Initials>JS</Initials><AffiliationInfo><Affiliation>Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, California 92037, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Saikatendu</LastName><ForeName>Kumar Singh</ForeName><Initials>KS</Initials></Author><Author ValidYN="Y"><LastName>Subramanian</LastName><ForeName>Vanitha</ForeName><Initials>V</Initials></Author><Author ValidYN="Y"><LastName>Neuman</LastName><ForeName>Benjamin W</ForeName><Initials>BW</Initials></Author><Author ValidYN="Y"><LastName>Brooun</LastName><ForeName>Alexei</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Griffith</LastName><ForeName>Mark</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Moy</LastName><ForeName>Kin</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Yadav</LastName><ForeName>Maneesh K</ForeName><Initials>MK</Initials></Author><Author ValidYN="Y"><LastName>Velasquez</LastName><ForeName>Jeffrey</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Buchmeier</LastName><ForeName>Michael J</ForeName><Initials>MJ</Initials></Author><Author ValidYN="Y"><LastName>Stevens</LastName><ForeName>Raymond C</ForeName><Initials>RC</Initials></Author><Author ValidYN="Y"><LastName>Kuhn</LastName><ForeName>Peter</ForeName><Initials>P</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>266200400058C</GrantID><Agency>PHS HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>Y1-CO-1020</GrantID><Acronym>CO</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>Y1-GM-1104</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Virol</MedlineTA><NlmUniqueID>0113724</NlmUniqueID><ISSNLinking>0022-538X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C558878">Nsp10 protein, SARS virus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017361">Viral Nonstructural Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017510" MajorTopicYN="N">Protein Folding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="Y">SARS Virus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017361" MajorTopicYN="N">Viral Nonstructural Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016335" MajorTopicYN="Y">Zinc Fingers</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>7</Month><Day>29</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2006</Year><Month>9</Month><Day>15</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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IdType="pubmed">9514967</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><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="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><name sortKey="Yadav, Maneesh K" sort="Yadav, Maneesh K" uniqKey="Yadav M" first="Maneesh K" last="Yadav">Maneesh K. Yadav</name></noCountry><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></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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