Crystal structure of the severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein dimerization domain reveals evolutionary linkage between corona- and arteriviridae.
Identifieur interne : 002239 ( PubMed/Checkpoint ); précédent : 002238; suivant : 002240Crystal structure of the severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein dimerization domain reveals evolutionary linkage between corona- and arteriviridae.
Auteurs : I-Mei Yu [États-Unis] ; Michael L. Oldham ; Jingqiang Zhang ; Jue ChenSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2006.
Descripteurs français
- KwdFr :
- Arteriviridae (génétique), Conformation des protéines, Cristallographie aux rayons X, Dimérisation, Données de séquences moléculaires, Liaison aux protéines, Protéines nucléocapside (), Similitude de séquences d'acides aminés, Structure tertiaire des protéines, Séquence d'acides aminés, Virus du SRAS (génétique), Virus du SRAS (métabolisme), Évolution moléculaire.
- MESH :
- génétique : Arteriviridae, Virus du SRAS.
- métabolisme : Virus du SRAS.
- Conformation des protéines, Cristallographie aux rayons X, Dimérisation, Données de séquences moléculaires, Liaison aux protéines, Protéines nucléocapside, Similitude de séquences d'acides aminés, Structure tertiaire des protéines, Séquence d'acides aminés, Évolution moléculaire.
English descriptors
- KwdEn :
- Amino Acid Sequence, Arteriviridae (genetics), Crystallography, X-Ray, Dimerization, Evolution, Molecular, Molecular Sequence Data, Nucleocapsid Proteins (chemistry), Protein Binding, Protein Conformation, Protein Structure, Tertiary, SARS Virus (genetics), SARS Virus (metabolism), Sequence Homology, Amino Acid.
- MESH :
- chemical , chemistry : Nucleocapsid Proteins.
- genetics : Arteriviridae, SARS Virus.
- metabolism : SARS Virus.
- Amino Acid Sequence, Crystallography, X-Ray, Dimerization, Evolution, Molecular, Molecular Sequence Data, Protein Binding, Protein Conformation, Protein Structure, Tertiary, Sequence Homology, Amino Acid.
Abstract
The causative agent of severe acute respiratory syndrome (SARS) is the SARS-associated coronavirus, SARS-CoV. The nucleocapsid (N) protein plays an essential role in SARS-CoV genome packaging and virion assembly. We have previously shown that SARS-CoV N protein forms a dimer in solution through its C-terminal domain. In this study, the crystal structure of the dimerization domain, consisting of residues 270-370, is determined to 1.75A resolution. The structure shows a dimer with extensive interactions between the two subunits, suggesting that the dimeric form of the N protein is the functional unit in vivo. Although lacking significant sequence similarity, the dimerization domain of SARS-CoV N protein has a fold similar to that of the nucleocapsid protein of the porcine reproductive and respiratory syndrome virus. This finding provides structural evidence of the evolutionary link between Coronaviridae and Arteriviridae, suggesting that the N proteins of both viruses have a common origin.
DOI: 10.1074/jbc.M602107200
PubMed: 16627473
Affiliations:
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Oldham</name></author><author><name sortKey="Zhang, Jingqiang" sort="Zhang, Jingqiang" uniqKey="Zhang J" first="Jingqiang" last="Zhang">Jingqiang Zhang</name></author><author><name sortKey="Chen, Jue" sort="Chen, Jue" uniqKey="Chen J" first="Jue" last="Chen">Jue Chen</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2006">2006</date><idno type="RBID">pubmed:16627473</idno><idno type="pmid">16627473</idno><idno type="doi">10.1074/jbc.M602107200</idno><idno type="wicri:Area/PubMed/Corpus">002266</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002266</idno><idno type="wicri:Area/PubMed/Curation">002266</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002266</idno><idno type="wicri:Area/PubMed/Checkpoint">002239</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002239</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Crystal structure of the severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein dimerization domain reveals evolutionary linkage between corona- and arteriviridae.</title><author><name sortKey="Yu, I Mei" sort="Yu, I Mei" uniqKey="Yu I" first="I-Mei" last="Yu">I-Mei Yu</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biological Sciences and the Cancer Center, Purdue University, West Lafayette, Indiana 47907, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Sciences and the Cancer Center, Purdue University, West Lafayette, Indiana 47907</wicri:regionArea><wicri:noRegion>Indiana 47907</wicri:noRegion></affiliation></author><author><name sortKey="Oldham, Michael L" sort="Oldham, Michael L" uniqKey="Oldham M" first="Michael L" last="Oldham">Michael L. Oldham</name></author><author><name sortKey="Zhang, Jingqiang" sort="Zhang, Jingqiang" uniqKey="Zhang J" first="Jingqiang" last="Zhang">Jingqiang Zhang</name></author><author><name sortKey="Chen, Jue" sort="Chen, Jue" uniqKey="Chen J" first="Jue" last="Chen">Jue Chen</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</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>Arteriviridae (genetics)</term><term>Crystallography, X-Ray</term><term>Dimerization</term><term>Evolution, Molecular</term><term>Molecular Sequence Data</term><term>Nucleocapsid Proteins (chemistry)</term><term>Protein Binding</term><term>Protein Conformation</term><term>Protein Structure, Tertiary</term><term>SARS Virus (genetics)</term><term>SARS Virus (metabolism)</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Arteriviridae (génétique)</term><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Dimérisation</term><term>Données de séquences moléculaires</term><term>Liaison aux protéines</term><term>Protéines nucléocapside ()</term><term>Similitude de séquences d'acides aminés</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Virus du SRAS (génétique)</term><term>Virus du SRAS (métabolisme)</term><term>Évolution moléculaire</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Nucleocapsid Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Arteriviridae</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Arteriviridae</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Crystallography, X-Ray</term><term>Dimerization</term><term>Evolution, Molecular</term><term>Molecular Sequence Data</term><term>Protein Binding</term><term>Protein Conformation</term><term>Protein Structure, Tertiary</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Dimérisation</term><term>Données de séquences moléculaires</term><term>Liaison aux protéines</term><term>Protéines nucléocapside</term><term>Similitude de séquences d'acides aminés</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Évolution moléculaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The causative agent of severe acute respiratory syndrome (SARS) is the SARS-associated coronavirus, SARS-CoV. The nucleocapsid (N) protein plays an essential role in SARS-CoV genome packaging and virion assembly. We have previously shown that SARS-CoV N protein forms a dimer in solution through its C-terminal domain. In this study, the crystal structure of the dimerization domain, consisting of residues 270-370, is determined to 1.75A resolution. The structure shows a dimer with extensive interactions between the two subunits, suggesting that the dimeric form of the N protein is the functional unit in vivo. Although lacking significant sequence similarity, the dimerization domain of SARS-CoV N protein has a fold similar to that of the nucleocapsid protein of the porcine reproductive and respiratory syndrome virus. This finding provides structural evidence of the evolutionary link between Coronaviridae and Arteriviridae, suggesting that the N proteins of both viruses have a common origin.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16627473</PMID><DateCompleted><Year>2006</Year><Month>08</Month><Day>11</Day></DateCompleted><DateRevised><Year>2007</Year><Month>11</Month><Day>14</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>281</Volume><Issue>25</Issue><PubDate><Year>2006</Year><Month>Jun</Month><Day>23</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J. Biol. Chem.</ISOAbbreviation></Journal><ArticleTitle>Crystal structure of the severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein dimerization domain reveals evolutionary linkage between corona- and arteriviridae.</ArticleTitle><Pagination><MedlinePgn>17134-9</MedlinePgn></Pagination><Abstract><AbstractText>The causative agent of severe acute respiratory syndrome (SARS) is the SARS-associated coronavirus, SARS-CoV. The nucleocapsid (N) protein plays an essential role in SARS-CoV genome packaging and virion assembly. We have previously shown that SARS-CoV N protein forms a dimer in solution through its C-terminal domain. In this study, the crystal structure of the dimerization domain, consisting of residues 270-370, is determined to 1.75A resolution. The structure shows a dimer with extensive interactions between the two subunits, suggesting that the dimeric form of the N protein is the functional unit in vivo. Although lacking significant sequence similarity, the dimerization domain of SARS-CoV N protein has a fold similar to that of the nucleocapsid protein of the porcine reproductive and respiratory syndrome virus. This finding provides structural evidence of the evolutionary link between Coronaviridae and Arteriviridae, suggesting that the N proteins of both viruses have a common origin.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yu</LastName><ForeName>I-Mei</ForeName><Initials>IM</Initials><AffiliationInfo><Affiliation>Department of Biological Sciences and the Cancer Center, Purdue University, West Lafayette, Indiana 47907, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Oldham</LastName><ForeName>Michael L</ForeName><Initials>ML</Initials></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Jingqiang</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Jue</ForeName><Initials>J</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>2GIB</AccessionNumber></AccessionNumberList></DataBank></DataBankList><GrantList CompleteYN="Y"><Grant><GrantID>P01 AI055672</GrantID><Acronym>AI</Acronym><Agency>NIAID 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><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2006</Year><Month>04</Month><Day>20</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019590">Nucleocapsid Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C099602">nucleocapsid protein, Coronavirus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D028382" MajorTopicYN="N">Arteriviridae</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019281" MajorTopicYN="N">Dimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019143" MajorTopicYN="N">Evolution, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019590" MajorTopicYN="N">Nucleocapsid Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>4</Month><Day>22</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2006</Year><Month>8</Month><Day>12</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2006</Year><Month>4</Month><Day>22</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16627473</ArticleId><ArticleId IdType="pii">M602107200</ArticleId><ArticleId IdType="doi">10.1074/jbc.M602107200</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Chen, Jue" sort="Chen, Jue" uniqKey="Chen J" first="Jue" last="Chen">Jue Chen</name><name sortKey="Oldham, Michael L" sort="Oldham, Michael L" uniqKey="Oldham M" first="Michael L" last="Oldham">Michael L. Oldham</name><name sortKey="Zhang, Jingqiang" sort="Zhang, Jingqiang" uniqKey="Zhang J" first="Jingqiang" last="Zhang">Jingqiang Zhang</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Yu, I Mei" sort="Yu, I Mei" uniqKey="Yu I" first="I-Mei" last="Yu">I-Mei Yu</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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