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.
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
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
Nat. Struct. Mol. Biol.
Date: Aug. 01, 2004
PubMed ID: 15235592
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