Structure of the Flavivirus helicase: implications for catalytic activity, protein interactions, and proteolytic processing

J Virol. 2005 Aug;79(16):10268-77. doi: 10.1128/JVI.79.16.10268-10277.2005.

Abstract

Yellow fever virus (YFV), a member of the Flavivirus genus, has a plus-sense RNA genome encoding a single polyprotein. Viral protein NS3 includes a protease and a helicase that are essential to virus replication and to RNA capping. The 1.8-A crystal structure of the helicase region of the YFV NS3 protein includes residues 187 to 623. Two familiar helicase domains bind nucleotide in a triphosphate pocket without base recognition, providing a site for nonspecific hydrolysis of nucleoside triphosphates and RNA triphosphate. The third, C-terminal domain has a unique structure and is proposed to function in RNA and protein recognition. The organization of the three domains indicates that cleavage of the viral polyprotein NS3-NS4A junction occurs in trans.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Amino Acid Sequence
  • Binding Sites
  • Catalysis
  • Flavivirus / enzymology*
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • RNA / metabolism
  • RNA Helicases / chemistry
  • RNA Helicases / physiology
  • Serine Endopeptidases / chemistry
  • Serine Endopeptidases / physiology
  • Viral Nonstructural Proteins / chemistry*
  • Viral Nonstructural Proteins / physiology
  • West Nile virus / enzymology*
  • Yellow fever virus / enzymology*

Substances

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