7XHJ

Crystal structure of RuvC from Deinococcus radiodurans

7XHJ の概要

• エントリーDOI: 10.2210/pdb7xhj/pdb
• 分子名称: Crossover junction endodeoxyribonuclease RuvC (2 entities in total)
• 機能のキーワード: nuclease, dna repair, homologous recombination, holliday junction resolvase, dna binding protein
• 由来する生物種: Deinococcus radiodurans ATCC 13939
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39363.68

構造登録者

Qin, C.,Zhao, Y. (登録日: 2022-04-08, 公開日: 2022-07-06, 最終更新日: 2023-11-29)

主引用文献

Qin, C.,Han, W.,Xu, Y.,Zhao, Y.,Xu, H.,Tian, B.,Wang, L.,Hua, Y.
Structural and Functional Characterization of the Holliday Junction Resolvase RuvC from Deinococcus radiodurans.
Microorganisms, 10:-, 2022

PubMed Abstract: Holliday junctions (HJs) are four-way DNA structures, which are an important intermediate in the process of homologous recombination. In most bacteria, HJs are cleaved by specific nucleases called RuvC resolvases at the end of homologous recombination. is an extraordinary radiation-resistant bacterium and is known as an ideal model organism for elucidating DNA repair processes. Here, we described the biochemical properties and the crystal structure of RuvC from (RuvC). RuvC exhibited an RNase H fold that belonged to the retroviral integrase family. Among many DNA substrates, RuvC specifically bound to HJ DNA and cleaved it. In particular, Mn was the preferred bivalent metal co-factor for HJ cleavage, whereas high concentrations of Mg inhibited the binding of RuvC to HJ. In addition, RuvC was crystallized and the crystals diffracted to 1.6 Å. The crystal structure of RuvC revealed essential amino acid sites for cleavage and binding activities, indicating that RuvC was a typical resolvase with a characteristic choice for metal co-factor.

PubMed: 35744678
DOI: 10.3390/microorganisms10061160

実験手法

X-RAY DIFFRACTION (1.6 Å)