2ZUC
Crystal structure of left-handed RadA filament
2ZUC の概要
エントリーDOI | 10.2210/pdb2zuc/pdb |
関連するPDBエントリー | 2DFL 2ZUB 2ZUD |
分子名称 | DNA repair and recombination protein radA (2 entities in total) |
機能のキーワード | archaea, filament, left-handed, dna binding, recombination, molecular switch, reca, rad51, dmc1, atp-binding, dna damage, dna recombination, dna-binding, nucleotide-binding |
由来する生物種 | Sulfolobus solfataricus |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 71828.06 |
構造登録者 | |
主引用文献 | Chang, Y.W.,Ko, T.P.,Lee, C.D.,Chang, Y.C.,Lin, K.A.,Chang, C.S.,Wang, A.H.J.,Wang, T.F. Three new structures of left-handed RADA helical filaments: structural flexibility of N-terminal domain is critical for recombinase activity Plos One, 4:e4890-e4890, 2009 Cited by PubMed Abstract: RecA family proteins, including bacterial RecA, archaeal RadA, and eukaryotic Dmc1 and Rad51, mediate homologous recombination, a reaction essential for maintaining genome integrity. In the presence of ATP, these proteins bind a single-strand DNA to form a right-handed nucleoprotein filament, which catalyzes pairing and strand exchange with a homologous double-stranded DNA (dsDNA), by as-yet unknown mechanisms. We recently reported a structure of RadA left-handed helical filament, and here present three new structures of RadA left-handed helical filaments. Comparative structural analysis between different RadA/Rad51 helical filaments reveals that the N-terminal domain (NTD) of RadA/Rad51, implicated in dsDNA binding, is highly flexible. We identify a hinge region between NTD and polymerization motif as responsible for rigid body movement of NTD. Mutant analysis further confirms that structural flexibility of NTD is essential for RadA's recombinase activity. These results support our previous hypothesis that ATP-dependent axial rotation of RadA nucleoprotein helical filament promotes homologous recombination. PubMed: 19295907DOI: 10.1371/journal.pone.0004890 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.3 Å) |
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