1T4G

ATPase in complex with AMP-PNP

1T4G の概要

• エントリーDOI: 10.2210/pdb1t4g/pdb
• 関連するPDBエントリー: 1PZN
• 分子名称: DNA repair and recombination protein radA, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 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: 35753.74

構造登録者

Wu, Y.,He, Y.,Moya, I.A.,Qian, X.,Luo, Y. (登録日: 2004-04-29, 公開日: 2004-08-17, 最終更新日: 2023-08-23)

主引用文献

Wu, Y.,He, Y.,Moya, I.A.,Qian, X.,Luo, Y.
Crystal Structure of Archaeal Recombinase RadA; A Snapshot of Its Extended Conformation.
Mol.Cell, 15:423-435, 2004

PubMed Abstract: Homologous recombination of DNA plays crucial roles in repairing severe DNA damage and in generating genetic diversity. The process is facilitated by a superfamily of recombinases: bacterial RecA, archaeal RadA and Rad51, and eukaryal Rad51 and DMC1. These recombinases share a common ATP-dependent filamentous quaternary structure for binding DNA and facilitating strand exchange. We have determined the crystal structure of Methanococcus voltae RadA in complex with the ATP analog AMP-PNP at 2.0 A resolution. The RadA filament is a 106.7 A pitch helix with six subunits per turn. The DNA binding loops L1 and L2 are located in close proximity to the filament axis. The ATP analog is buried between two RadA subunits, a feature similar to that of the active filament of Escherichia coli RecA revealed by electron microscopy. The disposition of the N-terminal domain suggests a role of the Helix-hairpin-Helix motif in binding double-stranded DNA.

PubMed: 15304222
DOI: 10.1016/j.molcel.2004.07.014

実験手法

X-RAY DIFFRACTION (2 Å)