4YOT

Crystal structure of a trimeric exonuclease PhoExo I from Pyrococcus horikoshii OT3 at 2.15A resolution

4YOT の概要

• エントリーDOI: 10.2210/pdb4yot/pdb
• 関連するPDBエントリー: 4YOR 4YOU 4YOV 4YOW 4YOX 4YOY
• 分子名称: 3-5 exonuclease PhoExo I, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: exonuclease, hydrolase
• 由来する生物種: Pyrococcus horikoshii
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 77075.95

構造登録者

Miyazono, K.,Tsutsumi, K.,Tanokura, M. (登録日: 2015-03-12, 公開日: 2015-07-15, 最終更新日: 2024-03-20)

主引用文献

Miyazono, K.,Ishino, S.,Tsutsumi, K.,Ito, T.,Ishino, Y.,Tanokura, M.
Structural basis for substrate recognition and processive cleavage mechanisms of the trimeric exonuclease PhoExo I
Nucleic Acids Res., 43:7122-7136, 2015

PubMed Abstract: Nucleases play important roles in nucleic acid processes, such as replication, repair and recombination. Recently, we identified a novel single-strand specific 3'-5' exonuclease, PfuExo I, from the hyperthermophilic archaeon Pyrococcus furiosus, which may be involved in the Thermococcales-specific DNA repair system. PfuExo I forms a trimer and cleaves single-stranded DNA at every two nucleotides. Here, we report the structural basis for the cleavage mechanism of this novel exonuclease family. A structural analysis of PhoExo I, the homologous enzyme from P. horikoshii OT3, showed that PhoExo I utilizes an RNase H-like active site and possesses a 3'-OH recognition site ∼9 Å away from the active site, which enables cleavage at every two nucleotides. Analyses of the heterotrimeric and monomeric PhoExo I activities showed that trimerization is indispensable for its processive cleavage mechanism, but only one active site of the trimer is required.

PubMed: 26138487
DOI: 10.1093/nar/gkv654

実験手法

X-RAY DIFFRACTION (2.15 Å)