3MWH

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

Summary for 3MWH

• Entry DOI: 10.2210/pdb3mwh/pdb
• Related: 3KGK
• Descriptor: Arsenical resistance operon trans-acting repressor arsD, GLYCEROL (3 entities in total)
• Functional Keywords: alpha+beta, arsenical resistance, chaperone, repressor, transcription, transcription regulation
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 24133.99

Authors

Ye, J.,Ajees, A.A.,Yang, J.,Rosen, B.P. (deposition date: 2010-05-05, release date: 2010-05-26, Last modification date: 2024-02-07)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.05 Å)