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

Acta Crystallogr Sect F Struct Biol Cryst Commun

Département de Virologie Structurale, Architecture et Fonction des Macromolécules Biologiques, UMR 6098, 163 Avenue de Luminy, 13288 Marseille CEDEX 09, France.

Published: March 2011

AI Article Synopsis

  • SARS coronavirus is the only known highly pathogenic human coronavirus, causing a 2003 outbreak with a 10% fatality rate.
  • Nsp16, a crucial protein for viral mRNA cap formation, functions as a methyltransferase but lacks known crystal structure.
  • This paper details the expression, purification, and crystallization of nsp10 in complex with nsp16, achieving crystals that diffracted to 1.9 Å resolution, with structure determination ongoing.

Article 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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3053173PMC
http://dx.doi.org/10.1107/S1744309111002867DOI Listing

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