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 RIS Download
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