Inhibition of Escherichia coli RecA by rationally redesigned N-terminal helix

Org Biomol Chem. 2007 May 21;5(10):1525-8. doi: 10.1039/b703159a. Epub 2007 Apr 18.

Abstract

Bacterial RecA promotes the development and transmission of antibiotic resistance genes by self-assembling into an ATP-hydrolyzing filamentous homopolymer on single-stranded DNA. We report the design of a 29mer peptide based on the RecA N-terminal domain involved in intermonomer contact that inhibits RecA filament assembly with an IC50 of 3 microM.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Adenosine Triphosphatases / chemistry
  • Adenosine Triphosphate / chemistry
  • Amino Acid Sequence
  • Chemistry, Pharmaceutical / methods
  • DNA, Single-Stranded / metabolism
  • Enzyme Inhibitors / chemical synthesis*
  • Enzyme Inhibitors / chemistry
  • Escherichia coli / enzymology*
  • Inhibitory Concentration 50
  • Models, Biological
  • Molecular Sequence Data
  • Polymers / chemistry
  • Protein Conformation
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Rec A Recombinases / antagonists & inhibitors*

Substances

  • DNA, Single-Stranded
  • Enzyme Inhibitors
  • Polymers
  • Adenosine Triphosphate
  • Rec A Recombinases
  • Adenosine Triphosphatases