1SZP

A Crystal Structure of the Rad51 Filament

1SZP の概要

• エントリーDOI: 10.2210/pdb1szp/pdb
• 分子名称: DNA repair protein RAD51, SULFATE ION (2 entities in total)
• 機能のキーワード: homologous recombination, asymmetry, rad51 filament, dna binding protein
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Nucleus: P25454
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 209988.61

構造登録者

Conway, A.B.,Lynch, T.W.,Zhang, Y.,Fortin, G.S.,Symington, L.S.,Rice, P.A. (登録日: 2004-04-06, 公開日: 2004-07-13, 最終更新日: 2023-08-23)

主引用文献

Conway, A.B.,Lynch, T.W.,Zhang, Y.,Fortin, G.S.,Fung, C.W.,Symington, L.S.,Rice, P.A.
Crystal structure of a Rad51 filament.
Nat.Struct.Mol.Biol., 11:791-796, 2004

PubMed Abstract: 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: 15235592
DOI: 10.1038/nsmb795

実験手法

X-RAY DIFFRACTION (3.25 Å)