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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

Authors

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

Journal

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