2GDJ

Delta-62 RADA recombinase in complex with AMP-PNP and magnesium

2GDJ の概要

• エントリーDOI: 10.2210/pdb2gdj/pdb
• 関連するPDBエントリー: 1T4G
• 分子名称: DNA repair and recombination protein radA, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (3 entities in total)
• 機能のキーワード: atpase, protein-atp complex, recombination
• 由来する生物種: Methanococcus voltae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29720.83

構造登録者

Wu, Y.,Qian, X.,He, Y.,Luo, Y. (登録日: 2006-03-16, 公開日: 2006-05-16, 最終更新日: 2023-08-30)

主引用文献

Galkin, V.E.,Wu, Y.,Zhang, X.-P.,Qian, X.,He, Y.,Yu, X.,Heyer, W.-D.,Luo, Y.,Egelman, E.H.
The Rad51/RadA N-Terminal Domain Activates Nucleoprotein Filament ATPase Activity.
Structure, 14:983-992, 2006

PubMed Abstract: Proteins in the RecA/RadA/Rad51 family form helical filaments on DNA that function in homologous recombination. While these proteins all have the same highly conserved ATP binding core, the RadA/Rad51 proteins have an N-terminal domain that shows no homology with the C-terminal domain found in RecA. Both the Rad51 N-terminal and RecA C-terminal domains have been shown to bind DNA, but no role for these domains has been established. We show that RadA filaments can be trapped in either an inactive or active conformation with respect to the ATPase and that activation involves a large rotation of the subunit aided by the N-terminal domain. The G103E mutation within the yeast Rad51 N-terminal domain inactivates the filament by failing to make proper contacts between the N-terminal domain and the core. These results show that the N-terminal domains play a regulatory role in filament activation and highlight the modular architecture of the recombination proteins.

PubMed: 16765891
DOI: 10.1016/j.str.2006.04.001

実験手法

X-RAY DIFFRACTION (2.5 Å)