Crystallization and diffraction analysis of the SARS coronavirus nsp10-nsp16 complex

被引：12

作者：

Debarnot, Claire ^{[1
]}

Imbert, Isabelle ^{[1
]}

Ferron, Francois ^{[1
]}

Gluais, Laure ^{[1
]}

Varlet, Isabelle ^{[1
]}

Papageorgiou, Nicolas ^{[1
]}

Bouvet, Mickael ^{[1
]}

Lescar, Julien ^{[1
,2
]}

Decroly, Etienne ^{[1
]}

Canard, Bruno ^{[1
]}

机构：

[1] Dept Virol Struct, UMR 6098, F-13288 Marseille 09, France

[2] Nanyang Technol Univ, Sch Biol Sci, Singapore 637551, Singapore

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2011年 / 67卷

关键词：

SARS coronavirus; nsp10; nsp16; MAGNETIC-RESONANCE STRUCTURE; CRYSTAL-STRUCTURE; BINDING; FOLD; TRANSCRIPTION; REVEALS; GENOME; UNIQUE; DOMAIN;

D O I：

10.1107/S1744309111002867

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 A resolution and crystal structure determination is in progress.

引用

页码：404 / 408

页数：5

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