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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Mar 1;67(Pt 3):404-8. doi: 10.1107/S1744309111002867. Epub 2011 Feb 25.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • Humans
  • Methyltransferases / chemistry*
  • Molecular Sequence Data
  • RNA-Dependent RNA Polymerase / chemistry*
  • RNA-Dependent RNA Polymerase / genetics
  • RNA-Dependent RNA Polymerase / isolation & purification
  • Severe acute respiratory syndrome-related coronavirus / chemistry*
  • Viral Nonstructural Proteins / chemistry*
  • Viral Nonstructural Proteins / genetics
  • Viral Nonstructural Proteins / isolation & purification

Substances

  • Nsp10 protein, SARS virus
  • Viral Nonstructural Proteins
  • Methyltransferases
  • Nsp16 protein, SARS virus
  • RNA-Dependent RNA Polymerase