2MYU

An arsenate reductase in oxidized state

2MYU の概要

• エントリーDOI: 10.2210/pdb2myu/pdb
• 関連するPDBエントリー: 2MYN 2MYP 2MYT
• NMR情報: BMRB: 25243
• 分子名称: Glutaredoxin arsenate reductase (1 entity in total)
• 機能のキーワード: alpha/beta/alpha sandwich fold, oxidoreductase
• 由来する生物種: Synechocystis sp.
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14409.24

構造登録者

Jin, C.,Hu, C.,Hu, Y. (登録日: 2015-01-30, 公開日: 2015-08-05, 最終更新日: 2024-11-20)

主引用文献

Hu, C.,Yu, C.,Liu, Y.,Hou, X.,Liu, X.,Hu, Y.,Jin, C.
A Hybrid Mechanism for the Synechocystis Arsenate Reductase Revealed by Structural Snapshots during Arsenate Reduction.
J.Biol.Chem., 290:22262-22273, 2015

PubMed Abstract: Evolution of enzymes plays a crucial role in obtaining new biological functions for all life forms. Arsenate reductases (ArsC) are several families of arsenic detoxification enzymes that reduce arsenate to arsenite, which can subsequently be extruded from cells by specific transporters. Among these, the Synechocystis ArsC (SynArsC) is structurally homologous to the well characterized thioredoxin (Trx)-coupled ArsC family but requires the glutaredoxin (Grx) system for its reactivation, therefore classified as a unique Trx/Grx-hybrid family. The detailed catalytic mechanism of SynArsC is unclear and how the "hybrid" mechanism evolved remains enigmatic. Herein, we report the molecular mechanism of SynArsC by biochemical and structural studies. Our work demonstrates that arsenate reduction is carried out via an intramolecular thiol-disulfide cascade similar to the Trx-coupled family, whereas the enzyme reactivation step is diverted to the coupling of the glutathione-Grx pathway due to the local structural difference. The current results support the hypothesis that SynArsC is likely a molecular fossil representing an intermediate stage during the evolution of the Trx-coupled ArsC family from the low molecular weight protein phosphotyrosine phosphatase (LMW-PTPase) family.

PubMed: 26224634
DOI: 10.1074/jbc.M115.659896

実験手法

SOLUTION NMR