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

Identifieur interne : 000124 ( Hal/Checkpoint ); précédent : 000123; suivant : 000125

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

Auteurs : Claire Debarnot [France] ; Isabelle Imbert ; François Ferron ; Laure Gluais ; Isabelle Varlet [France] ; Nicolas Papageorgiou ; Mickaël Bouvet [France] ; Julien Lescar ; Etienne Decroly [France] ; Bruno Canard

Source :

RBID : Hal:hal-00751530

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.


Url:
DOI: 10.1107/S1744309111002867

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Hal:hal-00751530

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