5X4J

The crystal structure of Pyrococcus furiosus RecJ (Zn-soaking)

5X4J の概要

• エントリーDOI: 10.2210/pdb5x4j/pdb
• 関連するPDBエントリー: 5X4H 5X4I 5X4K
• 分子名称: Uncharacterized protein, ZINC ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: archaeal recj, cmg interaction domain, nuclease activity, gins, interaction, hydrolase
• 由来する生物種: Pyrococcus furiosus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 56677.02

構造登録者

Li, M.J.,Yi, G.S.,Yu, F.,Zhou, H.,Chen, J.N.,Xu, C.Y.,Wang, F.P.,Xiao, X.,He, J.H.,Liu, X.P. (登録日: 2017-02-13, 公開日: 2018-02-14, 最終更新日: 2024-11-20)

主引用文献

Li, M.J.,Yi, G.S.,Yu, F.,Zhou, H.,Chen, J.N.,Xu, C.Y.,Wang, F.P.,Xiao, X.,He, J.H.,Liu, X.P.
The crystal structure of Pyrococcus furiosus RecJ implicates it as an ancestor of eukaryotic Cdc45.
Nucleic Acids Res., 45:12551-12564, 2017

PubMed Abstract: RecJ nucleases specifically degrade single-stranded (ss) DNA in the 5' to 3' direction. Archaeal RecJ is different from bacterial RecJ in sequence, domain organization, and substrate specificity. The RecJ from archaea Pyrococcus furiosus (PfuRecJ) also hydrolyzes RNA strands in the 3' to 5' direction. Like eukaryotic Cdc45 protein, archaeal RecJ forms a complex with MCM helicase and GINS. Here, we report the crystal structures of PfuRecJ and the complex of PfuRecJ and two CMPs. PfuRecJ bind one or two divalent metal ions in its crystal structure. A channel consisting of several positively charged residues is identified in the complex structure, and might be responsible for binding substrate ssDNA and/or releasing single nucleotide products. The deletion of the complex interaction domain (CID) increases the values of kcat/Km of 5' exonuclease activity on ssDNA and 3' exonuclease activity on ssRNA by 5- and 4-fold, respectively, indicating that the CID functions as a regulator of enzymatic activity. The DHH domain of PfuRecJ interacts with the C-terminal beta-sheet domain of the GINS51 subunit in the tetrameric GINS complex. The relationship of archaeal and bacterial RecJs, as well as eukaryotic Cdc45, is discussed based on biochemical and structural results.

PubMed: 30053256
DOI: 10.1093/nar/gkx887

実験手法

X-RAY DIFFRACTION (2.04 Å)