Dodecamer structure of severe acute respiratory syndrome coronavirus nonstructural protein nsp10.
Identifieur interne : 002153 ( PubMed/Corpus ); précédent : 002152; suivant : 002154Dodecamer structure of severe acute respiratory syndrome coronavirus nonstructural protein nsp10.
Auteurs : Dan Su ; Zhiyong Lou ; Fei Sun ; Yujia Zhai ; Haitao Yang ; Rongguang Zhang ; Andrzej Joachimiak ; Xuejun C. Zhang ; Mark Bartlam ; Zihe RaoSource :
- Journal of virology [ 0022-538X ] ; 2006.
English descriptors
- KwdEn :
- Amino Acid Sequence, Crystallography, X-Ray, Molecular Sequence Data, Protein Conformation, Protein Folding, SARS Virus (genetics), SARS Virus (physiology), Transcription Factors (chemistry), Transcription Factors (genetics), Transcription Factors (physiology), Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (physiology), Zinc Fingers.
- MESH :
- chemical , chemistry : Transcription Factors, Viral Nonstructural Proteins.
- genetics : SARS Virus, Transcription Factors, Viral Nonstructural Proteins.
- physiology : SARS Virus, Transcription Factors, Viral Nonstructural Proteins.
- Amino Acid Sequence, Crystallography, X-Ray, Molecular Sequence Data, Protein Conformation, Protein Folding, Zinc Fingers.
Abstract
The severe acute respiratory syndrome coronavirus (SARS-CoV) nonstructural proteins nsp1 to nsp16 have been implicated by genetic analysis in the assembly of a functional replication/transcription complex. We report the crystal structure of nsp10 from SARS-CoV at 2.1-A resolution. The nsp10 structure has a novel fold, and 12 identical subunits assemble to form a unique spherical dodecameric architecture. Two zinc fingers have been identified from the nsp10 monomer structure with the sequence motifs C-(X)2-C-(X)5-H-(X)6-C and C-(X)2-C-(X)7-C-(X)-C. The nsp10 crystal structure is the first of a new class of zinc finger protein three-dimensional structures to be revealed experimentally. The zinc finger sequence motifs are conserved among all three coronavirus antigenic groups, implicating an essential function for nsp10 in all coronaviruses. Based on the structure, we propose that nsp10 is a transcription factor for coronavirus replication/transcription.
DOI: 10.1128/JVI.00483-06
PubMed: 16873247
Links to Exploration step
pubmed:16873247Le document en format XML
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Zhang</name></author><author><name sortKey="Bartlam, Mark" sort="Bartlam, Mark" uniqKey="Bartlam M" first="Mark" last="Bartlam">Mark Bartlam</name></author><author><name sortKey="Rao, Zihe" sort="Rao, Zihe" uniqKey="Rao Z" first="Zihe" last="Rao">Zihe Rao</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2006">2006</date><idno type="RBID">pubmed:16873247</idno><idno type="pmid">16873247</idno><idno type="doi">10.1128/JVI.00483-06</idno><idno type="wicri:Area/PubMed/Corpus">002153</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002153</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Dodecamer structure of severe acute respiratory syndrome coronavirus nonstructural protein nsp10.</title><author><name sortKey="Su, Dan" sort="Su, Dan" uniqKey="Su D" first="Dan" last="Su">Dan Su</name><affiliation><nlm:affiliation>Tsinghua-IBP Joint Research Group for Structural Biology, Tsinghua University, Beijing 100084, China.</nlm:affiliation></affiliation></author><author><name sortKey="Lou, Zhiyong" sort="Lou, Zhiyong" uniqKey="Lou Z" first="Zhiyong" last="Lou">Zhiyong Lou</name></author><author><name sortKey="Sun, Fei" sort="Sun, Fei" uniqKey="Sun F" first="Fei" last="Sun">Fei Sun</name></author><author><name sortKey="Zhai, Yujia" sort="Zhai, Yujia" uniqKey="Zhai Y" first="Yujia" last="Zhai">Yujia Zhai</name></author><author><name sortKey="Yang, Haitao" sort="Yang, Haitao" uniqKey="Yang H" first="Haitao" last="Yang">Haitao Yang</name></author><author><name sortKey="Zhang, Rongguang" sort="Zhang, Rongguang" uniqKey="Zhang R" first="Rongguang" last="Zhang">Rongguang Zhang</name></author><author><name sortKey="Joachimiak, Andrzej" sort="Joachimiak, Andrzej" uniqKey="Joachimiak A" first="Andrzej" last="Joachimiak">Andrzej Joachimiak</name></author><author><name sortKey="Zhang, Xuejun C" sort="Zhang, Xuejun C" uniqKey="Zhang X" first="Xuejun C" last="Zhang">Xuejun C. Zhang</name></author><author><name sortKey="Bartlam, Mark" sort="Bartlam, Mark" uniqKey="Bartlam M" first="Mark" last="Bartlam">Mark Bartlam</name></author><author><name sortKey="Rao, Zihe" sort="Rao, Zihe" uniqKey="Rao Z" first="Zihe" last="Rao">Zihe Rao</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 (genetics)</term><term>SARS Virus (physiology)</term><term>Transcription Factors (chemistry)</term><term>Transcription Factors (genetics)</term><term>Transcription Factors (physiology)</term><term>Viral Nonstructural Proteins (chemistry)</term><term>Viral Nonstructural Proteins (genetics)</term><term>Viral Nonstructural Proteins (physiology)</term><term>Zinc Fingers</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Transcription Factors</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term><term>Transcription Factors</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term><term>Transcription Factors</term><term>Viral Nonstructural Proteins</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>Zinc Fingers</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The severe acute respiratory syndrome coronavirus (SARS-CoV) nonstructural proteins nsp1 to nsp16 have been implicated by genetic analysis in the assembly of a functional replication/transcription complex. We report the crystal structure of nsp10 from SARS-CoV at 2.1-A resolution. The nsp10 structure has a novel fold, and 12 identical subunits assemble to form a unique spherical dodecameric architecture. Two zinc fingers have been identified from the nsp10 monomer structure with the sequence motifs C-(X)2-C-(X)5-H-(X)6-C and C-(X)2-C-(X)7-C-(X)-C. The nsp10 crystal structure is the first of a new class of zinc finger protein three-dimensional structures to be revealed experimentally. The zinc finger sequence motifs are conserved among all three coronavirus antigenic groups, implicating an essential function for nsp10 in all coronaviruses. Based on the structure, we propose that nsp10 is a transcription factor for coronavirus replication/transcription.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16873247</PMID><DateCompleted><Year>2006</Year><Month>09</Month><Day>14</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</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>Dodecamer structure of severe acute respiratory syndrome coronavirus nonstructural protein nsp10.</ArticleTitle><Pagination><MedlinePgn>7902-8</MedlinePgn></Pagination><Abstract><AbstractText>The severe acute respiratory syndrome coronavirus (SARS-CoV) nonstructural proteins nsp1 to nsp16 have been implicated by genetic analysis in the assembly of a functional replication/transcription complex. We report the crystal structure of nsp10 from SARS-CoV at 2.1-A resolution. The nsp10 structure has a novel fold, and 12 identical subunits assemble to form a unique spherical dodecameric architecture. Two zinc fingers have been identified from the nsp10 monomer structure with the sequence motifs C-(X)2-C-(X)5-H-(X)6-C and C-(X)2-C-(X)7-C-(X)-C. The nsp10 crystal structure is the first of a new class of zinc finger protein three-dimensional structures to be revealed experimentally. The zinc finger sequence motifs are conserved among all three coronavirus antigenic groups, implicating an essential function for nsp10 in all coronaviruses. Based on the structure, we propose that nsp10 is a transcription factor for coronavirus replication/transcription.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Su</LastName><ForeName>Dan</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Tsinghua-IBP Joint Research Group for Structural Biology, Tsinghua University, Beijing 100084, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lou</LastName><ForeName>Zhiyong</ForeName><Initials>Z</Initials></Author><Author ValidYN="Y"><LastName>Sun</LastName><ForeName>Fei</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Zhai</LastName><ForeName>Yujia</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Haitao</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Rongguang</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Joachimiak</LastName><ForeName>Andrzej</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Xuejun C</ForeName><Initials>XC</Initials></Author><Author ValidYN="Y"><LastName>Bartlam</LastName><ForeName>Mark</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Rao</LastName><ForeName>Zihe</ForeName><Initials>Z</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</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="D014157">Transcription 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MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014157" MajorTopicYN="N">Transcription Factors</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017361" MajorTopicYN="N">Viral Nonstructural Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016335" MajorTopicYN="Y">Zinc Fingers</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate 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