3KGK
Crystal structure of ArsD
Summary for 3KGK
| Entry DOI | 10.2210/pdb3kgk/pdb |
| Descriptor | Arsenical resistance operon trans-acting repressor arsD (2 entities in total) |
| Functional Keywords | alpha+beta, arsenical resistance, chaperone, dna-binding, repressor, transcription, transcription regulation |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 23881.51 |
| Authors | Ye, J.,Rosen, B.P. (deposition date: 2009-10-29, release date: 2010-02-16, 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 Cited by 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: 20507177DOI: 10.1021/bi100571r PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
Download full validation report
