1JL3

Crystal Structure of B. subtilis ArsC

1JL3 の概要

• エントリーDOI: 10.2210/pdb1jl3/pdb
• 分子名称: ARSENATE REDUCTASE, SULFATE ION (3 entities in total)
• 機能のキーワード: alpha-beta fold, ptp-loop, arsenate reductase, oxidoreductase
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cytoplasm : P45947
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 62842.17

構造登録者

Su, X.-D.,Bennett, M.S. (登録日: 2001-07-15, 公開日: 2001-10-24, 最終更新日: 2024-02-07)

主引用文献

Bennett, M.S.,Guan, Z.,Laurberg, M.,Su, X.D.
Bacillus subtilis arsenate reductase is structurally and functionally similar to low molecular weight protein tyrosine phosphatases.
Proc.Natl.Acad.Sci.USA, 98:13577-13582, 2001

PubMed Abstract: Arsenate is an abundant oxyanion that, because of its ability to mimic the phosphate group, is toxic to cells. Arsenate reductase (EC; encoded by the arsC gene in bacteria) participates to achieve arsenate resistance in both prokaryotes and yeast by reducing arsenate to arsenite; the arsenite is then exported by a specific transporter. The crystal structure of Bacillus subtilis arsenate reductase in the reduced form with a bound sulfate ion in its active site is solved at 1.6-A resolution. Significant structural similarity is seen between arsenate reductase and bovine low molecular weight protein tyrosine phosphatase, despite very low sequence identity. The similarity is especially high between their active sites. It is further confirmed that this structural homology is relevant functionally by showing the phosphatase activity of the arsenate reductase in vitro. Thus, we can understand the arsenate reduction in the light of low molecular weight protein tyrosine phosphatase mechanism and also explain the catalytic roles of essential residues such as Cys-10, Cys-82, Cys-89, Arg-16, and Asp-105. A "triple cysteine redox relay" is proposed for the arsenate reduction mechanism.

PubMed: 11698660
DOI: 10.1073/pnas.241397198

実験手法

X-RAY DIFFRACTION (1.6 Å)