1szp
From Proteopedia
A Crystal Structure of the Rad51 Filament
Structural highlights
FunctionRAD51_YEAST Required both for recombination and for the repair of DNA damage caused by X-rays. Its function may be modulated by interaction with other repair proteins. RAD52 interacts directly with RAD51, via its C-terminus. Forms a nucleoprotein filament with DNA as an early intermediate in recombination.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedRad51, 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. Crystal structure of a Rad51 filament.,Conway AB, Lynch TW, Zhang Y, Fortin GS, Fung CW, Symington LS, Rice PA Nat Struct Mol Biol. 2004 Aug;11(8):791-6. Epub 2004 Jul 4. PMID:15235592[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
