Crystallization and diffraction analysis of the SARS coronavirus nsp10-nsp16 complex.
Identifieur interne : 001539 ( PubMed/Corpus ); précédent : 001538; suivant : 001540Crystallization and diffraction analysis of the SARS coronavirus nsp10-nsp16 complex.
Auteurs : Claire Debarnot ; Isabelle Imbert ; François Ferron ; Laure Gluais ; Isabelle Varlet ; Nicolas Papageorgiou ; Mickaël Bouvet ; Julien Lescar ; Etienne Decroly ; Bruno CanardSource :
- Acta crystallographica. Section F, Structural biology and crystallization communications [ 1744-3091 ] ; 2011.
English descriptors
- KwdEn :
- Cloning, Molecular, Crystallization, Crystallography, X-Ray, Humans, Methyltransferases (chemistry), Molecular Sequence Data, RNA Replicase (chemistry), RNA Replicase (genetics), RNA Replicase (isolation & purification), SARS Virus (chemistry), Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (isolation & purification).
- MESH :
- chemical , chemistry : Methyltransferases, RNA Replicase, Viral Nonstructural Proteins.
- chemical , genetics : RNA Replicase, Viral Nonstructural Proteins.
- chemical , isolation & purification : RNA Replicase, Viral Nonstructural Proteins.
- chemistry : SARS Virus.
- Cloning, Molecular, Crystallization, Crystallography, X-Ray, Humans, Molecular Sequence Data.
Abstract
To date, the SARS coronavirus is the only known highly pathogenic human coronavirus. In 2003, it was responsible for a large outbreak associated with a 10% fatality rate. This positive RNA virus encodes a large replicase polyprotein made up of 16 gene products (nsp1-16), amongst which two methyltransferases, nsp14 and nsp16, are involved in viral mRNA cap formation. The crystal structure of nsp16 is unknown. Nsp16 is an RNA-cap AdoMet-dependent (nucleoside-2'-O-)-methyltransferase that is only active in the presence of nsp10. In this paper, the expression, purification and crystallization of nsp10 in complex with nsp16 are reported. The crystals diffracted to a resolution of 1.9 Å resolution and crystal structure determination is in progress.
DOI: 10.1107/S1744309111002867
PubMed: 21393853
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pubmed:21393853Le document en format XML
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<term>Methyltransferases (chemistry)</term>
<term>Molecular Sequence Data</term>
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<term>RNA Replicase (genetics)</term>
<term>RNA Replicase (isolation & purification)</term>
<term>SARS Virus (chemistry)</term>
<term>Viral Nonstructural Proteins (chemistry)</term>
<term>Viral Nonstructural Proteins (genetics)</term>
<term>Viral Nonstructural Proteins (isolation & purification)</term>
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<front><div type="abstract" xml:lang="en">To date, the SARS coronavirus is the only known highly pathogenic human coronavirus. In 2003, it was responsible for a large outbreak associated with a 10% fatality rate. This positive RNA virus encodes a large replicase polyprotein made up of 16 gene products (nsp1-16), amongst which two methyltransferases, nsp14 and nsp16, are involved in viral mRNA cap formation. The crystal structure of nsp16 is unknown. Nsp16 is an RNA-cap AdoMet-dependent (nucleoside-2'-O-)-methyltransferase that is only active in the presence of nsp10. In this paper, the expression, purification and crystallization of nsp10 in complex with nsp16 are reported. The crystals diffracted to a resolution of 1.9 Å resolution and crystal structure determination is in progress.</div>
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<ReferenceList><Reference><Citation>J Virol. 2007 Apr;81(7):3151-61</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17202208</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 2003 Aug 29;331(5):991-1004</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12927536</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2006 Aug;80(16):7894-901</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16873246</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2009 Feb;83(4):1823-36</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19052085</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2004 Mar 16;101(11):3792-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15007178</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2006 Aug 8;103(32):11892-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16882730</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Struct Mol Biol. 2005 Nov;12(11):980-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16228002</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2006 Aug;80(16):7902-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16873247</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virus Res. 2008 May;133(2):136-48</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18255185</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2008 Aug;82(16):8071-84</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18417574</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 2010 Jan;91(Pt 1):112-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19776234</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2007 Jun;81(12):6700-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17409150</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2007 Nov;81(21):12049-60</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17728234</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 2003 Jun 13;113(6):701-2</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12809601</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2010 Oct 22;285(43):33230-41</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20699222</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1981 May;38(2):661-70</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6165837</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 2003 Sep;84(Pt 9):2305-15</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12917450</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 1994 Sep 1;50(Pt 5):760-3</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15299374</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2006 Sep;80(17):8493-502</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16912299</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 2006 Oct 18;25(20):4933-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17024178</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 2002 Dec 2;21(23):6571-80</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12456663</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>PLoS Pathog. 2010 Apr;6(4):e1000863</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20421945</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):125-32</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20124692</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 2002 Jul 1;21(13):3213-24</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12093723</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2006 Apr 11;103(15):5717-22</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16581910</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
</record>
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