ATP Hydrolysis in the RecA-DNA Filament Promotes Structural Changes at the Protein-DNA Interface

Biochemistry. 2015 Aug 4;54(30):4579-82. doi: 10.1021/acs.biochem.5b00614. Epub 2015 Jul 27.

Abstract

To address the mechanistic roles of ATP hydrolysis in RecA-promoted strand exchange reaction in homologous recombination, quantum mechanical calculations are performed on key parts of the RecA-DNA complex. We find that ATP hydrolysis may induce changes at the protein-DNA interface, resulting in the rearrangement of the hydrogen bond network connecting the ATP and the DNA binding sites.

Publication types

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

MeSH terms

  • Adenosine Triphosphate / chemistry*
  • Adenosine Triphosphate / metabolism
  • DNA, Single-Stranded / chemistry*
  • DNA, Single-Stranded / metabolism
  • Hydrolysis
  • Models, Chemical*
  • Rec A Recombinases / chemistry*
  • Rec A Recombinases / metabolism

Substances

  • DNA, Single-Stranded
  • Adenosine Triphosphate
  • Rec A Recombinases