Temporal and spatial control of the adenovirus proteinase by both a peptide and the viral DNA

Trends Biochem Sci. 1997 Oct;22(10):393-8. doi: 10.1016/s0968-0004(97)01123-7.

Abstract

The adenovirus proteinase (AVP) uses both an 11-amino acid peptide (pVIc) and the viral DNA as cofactors to increase its catalytic rate constant 6000-fold. The crystal structure of an AVP-pVIc complex at 2.6-A resolution reveals a new protein fold of an enzyme that is the first member of a new class of cysteine proteinases, which arose via convergent evolution.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Adenoviridae / enzymology*
  • Cysteine Endopeptidases / metabolism*
  • DNA, Viral / physiology*
  • Models, Molecular
  • Protein Structure, Secondary*
  • Time Factors

Substances

  • DNA, Viral
  • Cysteine Endopeptidases