2FCO

Crystal Structure of Bacillus stearothermophilus PrfA-Holliday Junction Resolvase

2FCO の概要

• エントリーDOI: 10.2210/pdb2fco/pdb
• 分子名称: recombination protein U (penicillin-binding protein related factor A), MAGNESIUM ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: flexibility, hydrolase
• 由来する生物種: Geobacillus kaustophilus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46317.13

構造登録者

Li, J.,Jedrzejas, M.J. (登録日: 2005-12-12, 公開日: 2006-11-21, 最終更新日: 2024-02-14)

主引用文献

Kelly, S.J.,Li, J.,Setlow, P.,Jedrzejas, M.J.
Structure, flexibility, and mechanism of the Bacillus stearothermophilus RecU Holliday junction resolvase.
Proteins, 68:961-971, 2007

PubMed Abstract: Here we report a high resolution structure of RecU-Holliday junction resolvase from Bacillus stearothermophilus. The functional unit of RecU is a homodimer that contains a "mushroom" like structure with a rigid cap and two highly flexible loops extending outwards. These loops appear to be highly flexible/dynamic, and presumably are directly involved in DNA binding and holding it for catalysis. Structural modifications of both the protein and DNA upon their interaction are essential for catalysis. An Mg2+ ion is present in each of the two active sites in this homodimeric enzyme, and two water molecules are coordinated with each Mg2+ ion. Our data are consistent with one of these water molecules acting as a nucleophile and the other as a general acid. The identities of the general base and general acid involved in catalysis and the Lewis acid that stabilizes the pentacovalent transition state phosphate ion are proposed. A model for the RecU-Holliday junction DNA complex is also proposed and discussed in the context of DNA binding and cleavage.

PubMed: 17557334
DOI: 10.1002/prot.21418

実験手法

X-RAY DIFFRACTION (1.4 Å)