Our hosting provider will be performing UPS maintenance on Tuesday, Oct 25, 2016 between 8 AM and 5 PM PDT. SciCrunch searching services will be down during this time.

Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

Crystal structure of a Rad51 filament.


Rad51, the major eukaryotic homologous recombinase, is important for the repair of DNA damage and the maintenance of genomic diversity and stability. The active form of this DNA-dependent ATPase is a helical filament within which the search for homology and strand exchange occurs. Here we present the crystal structure of a Saccharomyces cerevisiae Rad51 filament formed by a gain-of-function mutant. This filament has a longer pitch than that seen in crystals of Rad51's prokaryotic homolog RecA, and places the ATPase site directly at a new interface between protomers. Although the filament exhibits approximate six-fold symmetry, alternate protein-protein interfaces are slightly different, implying that the functional unit of Rad51 within the filament may be a dimer. Additionally, we show that mutation of His352, which lies at this new interface, markedly disrupts DNA binding.

Pubmed ID: 15235592


  • Conway AB
  • Lynch TW
  • Zhang Y
  • Fortin GS
  • Fung CW
  • Symington LS
  • Rice PA


Nature structural & molecular biology

Publication Data

August 28, 2004

Associated Grants

  • Agency: NIGMS NIH HHS, Id: 2 T32 GM008720
  • Agency: NIGMS NIH HHS, Id: GM058827
  • Agency: NIGMS NIH HHS, Id: GM54099
  • Agency: NCRR NIH HHS, Id: RR07707
  • Agency: NCI NIH HHS, Id: T32 CA09503
  • Agency: NCI NIH HHS, Id: T32 CA09594

Mesh Terms

  • Adenosine Triphosphatases
  • Adenosine Triphosphate
  • Crystallography, X-Ray
  • DNA
  • DNA Damage
  • DNA-Binding Proteins
  • Histidine
  • Hydrogen-Ion Concentration
  • Hydrolysis
  • Models, Molecular
  • Mutation
  • Phosphorylation
  • Protein Binding
  • Protein Conformation
  • Rad51 Recombinase
  • Rec A Recombinases
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Time Factors
  • Tyrosine