期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 11, 期 8, 页码 791-796出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb795
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资金
- NCI NIH HHS [T32 CA09594, T32 CA09503] Funding Source: Medline
- NCRR NIH HHS [RR07707] Funding Source: Medline
- NIGMS NIH HHS [GM54099, GM058827, 2 T32 GM008720] Funding Source: Medline
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.
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