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

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.

SUBMITTER: Debarnot C

PROVIDER: S-EPMC3053173 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature

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

Debarnot Claire C Imbert Isabelle I Ferron François F Gluais Laure L Varlet Isabelle I Papageorgiou Nicolas N Bouvet Mickaël M Lescar Julien J Decroly Etienne E Canard Bruno B

Acta crystallographica. Section F, Structural biology and crystallization communications 20110225 Pt 3

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 a ...[more]

PMID: 21393853

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Molecular Docking Studies to Identify Promising Natural Inhibitors Targeting SARS-CoV-2 Nsp10-Nsp16 Protein Complex

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| S-EPMC8892556 | biostudies-literature

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