Details

Autor(en) / Beteiligte

• Rice, Phoebe A
• Conway, Adam B
• Lynch, Thomas W
• Zhang, Ying
• Fortin, Gary S
• Fung, Cindy W
• Symington, Lorraine S

Titel

Crystal structure of a Rad51 filament

Ist Teil von

• Nature structural & molecular biology, 2004-08, Vol.11 (8), p.791-796

Ort / Verlag

United States: Nature Publishing Group

Erscheinungsjahr

2004

Quelle

MEDLINE

Beschreibungen/Notizen

• 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.