3MWH

The 1.4 Ang crystal structure of the ArsD arsenic metallochaperone provides insights into its interactions with the ArsA ATPase

3MWH の概要

• エントリーDOI: 10.2210/pdb3mwh/pdb
• 関連するPDBエントリー: 3KGK
• 分子名称: Arsenical resistance operon trans-acting repressor arsD, GLYCEROL (3 entities in total)
• 機能のキーワード: alpha+beta, arsenical resistance, chaperone, repressor, transcription, transcription regulation
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24133.99

構造登録者

Ye, J.,Ajees, A.A.,Yang, J.,Rosen, B.P. (登録日: 2010-05-05, 公開日: 2010-05-26, 最終更新日: 2024-02-07)

主引用文献

Ye, J.,Ajees, A.A.,Yang, J.,Rosen, B.P.
The 1.4 A crystal structure of the ArsD arsenic metallochaperone provides insights into its interaction with the ArsA ATPase.
Biochemistry, 49:5206-5212, 2010

PubMed Abstract: Arsenic is a carcinogen that tops the Superfund list of hazardous chemicals. Bacterial resistance to arsenic is facilitated by ArsD, which delivers As(III) to the ArsA ATPase, the catalytic subunit of the ArsAB pump. Here we report the structure of the arsenic metallochaperone ArsD at 1.4 A and a model for its binding of metalloid. There are two ArsD molecules in the asymmetric unit. The overall structure of the ArsD monomer has a thioredoxin fold, with a core of four beta-strands flanked by four alpha-helices. Based on data from structural homologues, ArsD was modeled with and without bound As(III). ArsD binds one arsenic per monomer coordinated with the three sulfur atoms of Cys12, Cys13, and Cys18. Using this structural model, an algorithm was used to dock ArsD and ArsA. The resulting docking model provides testable predictions of the contact points of the two proteins and forms the basis for future experiments.

PubMed: 20507177
DOI: 10.1021/bi100571r

実験手法

X-RAY DIFFRACTION (2.05 Å)