Structure of the Murray Valley encephalitis virus RNA helicase at 1.9 Angstrom resolution

Protein Sci. 2007 Oct;16(10):2294-300. doi: 10.1110/ps.072843107.

Abstract

Murray Valley encephalitis virus (MVEV), a mosquito-borne flavivirus endemic to Australia, is closely related to Japanese encephalitis virus and West Nile virus. Nonstructural protein 3 (NS3) is a multifunctional enzyme with serine protease and DEXH/D-box helicase domains, whose activity is central to flavivirus replication and is therefore a possible target for anti-flaviviral compounds. Cloning, purification, and crystal structure determination to 1.9 Angstrom resolution of the NS3 helicase of MVEV and characterization of its enzymatic activity is reported. Comparison with the structures of helicases from related viruses supports a possible mechanism of ATP hydrolysis-driven strand separation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Crystallography, X-Ray
  • Encephalitis Virus, Murray Valley / enzymology*
  • Models, Molecular*
  • Molecular Sequence Data
  • Nucleotides / chemistry
  • RNA Helicases / chemistry*
  • RNA Helicases / metabolism
  • Sequence Alignment
  • Serine Endopeptidases / chemistry
  • Serine Endopeptidases / metabolism
  • Viral Nonstructural Proteins / chemistry*
  • Viral Nonstructural Proteins / metabolism

Substances

  • NS3 protein, flavivirus
  • Nucleotides
  • Viral Nonstructural Proteins
  • Serine Endopeptidases
  • Adenosine Triphosphatases
  • RNA Helicases

Associated data

  • PDB/2V8O