1Z2E

Solution Structure of Bacillus subtilis ArsC in oxidized state

1Z2E の概要

• エントリーDOI: 10.2210/pdb1z2e/pdb
• 関連するPDBエントリー: 1JL3 1Z2D
• NMR情報: BMRB: 6075
• 分子名称: Arsenate reductase (1 entity in total)
• 機能のキーワード: bacillus subtilis, arsenate reductase, solution structure, structural genomics, oxidoreductase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15614.48

構造登録者

Jin, C.,Li, Y. (登録日: 2005-03-08, 公開日: 2005-10-04, 最終更新日: 2024-10-09)

主引用文献

Guo, X.,Li, Y.,Peng, K.,Hu, Y.,Li, C.,Xia, B.,Jin, C.
Solution Structures and Backbone Dynamics of Arsenate Reductase from Bacillus subtilis: REVERSIBLE CONFORMATIONAL SWITCH ASSOCIATED WITH ARSENATE REDUCTION
J.Biol.Chem., 280:39601-39608, 2005

PubMed Abstract: Arsenate reductase encoded by the chromosomal arsC gene in Bacillus subtilis catalyzes the intracellular reduction of arsenate to arsenite, which is then extruded from cells through an efficient and specific transport system. Herein, we present the solution structures and backbone dynamics of both the reduced and oxidized forms of arsenate reductase from B. subtilis. The overall structures of both forms are similar to those of bovine low molecular weight protein-tyrosine phosphatase and arsenate reductase from Staphylococcus aureus. However, several features of the tertiary structure and mobility are notably different between the reduced and oxidized forms of B. subtilis arsenate reductase, particularly in the P-loop region and the segment Cys(82)-Cys(89). The backbone dynamics results demonstrated that the reduced form of arsenate reductase undergoes millisecond conformational changes in the functional P-loop and Cys(82)-Cys(89), which may facilitate the formation of covalent intermediates and subsequent reduction of arsenate. In the oxidized form, Cys(82)-Cys(89) shows motional flexibility on both picosecond-to-nanosecond and possibly millisecond time scales, which may facilitate the reduction of the oxidized enzyme by thioredoxin to regenerate the active enzyme. Overall, the internal dynamics and static structures of the enzyme provide insights into the molecular mechanism of arsenate reduction, especially the reversible conformational switch and changes in internal motions associated with the catalytic reaction.

PubMed: 16192272
DOI: 10.1074/jbc.M508132200

実験手法

SOLUTION NMR