Crystal structure of the severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein dimerization domain reveals evolutionary linkage between corona- and arteriviridae.
Identifieur interne : 002266 ( PubMed/Corpus ); précédent : 002265; suivant : 002267Crystal structure of the severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein dimerization domain reveals evolutionary linkage between corona- and arteriviridae.
Auteurs : I-Mei Yu ; Michael L. Oldham ; Jingqiang Zhang ; Jue ChenSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2006.
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
Links to Exploration step
pubmed:16627473Le document en format XML
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<author><name sortKey="Yu, I Mei" sort="Yu, I Mei" uniqKey="Yu I" first="I-Mei" last="Yu">I-Mei Yu</name>
<affiliation><nlm:affiliation>Department of Biological Sciences and the Cancer Center, Purdue University, West Lafayette, Indiana 47907, USA.</nlm:affiliation>
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<author><name sortKey="Oldham, Michael L" sort="Oldham, Michael L" uniqKey="Oldham M" first="Michael L" last="Oldham">Michael L. Oldham</name>
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<author><name sortKey="Zhang, Jingqiang" sort="Zhang, Jingqiang" uniqKey="Zhang J" first="Jingqiang" last="Zhang">Jingqiang Zhang</name>
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<author><name sortKey="Chen, Jue" sort="Chen, Jue" uniqKey="Chen J" first="Jue" last="Chen">Jue Chen</name>
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<author><name sortKey="Yu, I Mei" sort="Yu, I Mei" uniqKey="Yu I" first="I-Mei" last="Yu">I-Mei Yu</name>
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<author><name sortKey="Zhang, Jingqiang" sort="Zhang, Jingqiang" uniqKey="Zhang J" first="Jingqiang" last="Zhang">Jingqiang Zhang</name>
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<author><name sortKey="Chen, Jue" sort="Chen, Jue" uniqKey="Chen J" first="Jue" last="Chen">Jue Chen</name>
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<series><title level="j">The Journal of biological chemistry</title>
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<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>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Nucleocapsid Proteins</term>
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<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>
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<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>
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<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>
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