The 1.4 Å crystal structure of the arsd arsenic metallochaperone provides insights into its interaction with the ArsA ATPase

Jun Ye, A. Abdul Ajees, Jianbo Yang, Barry P. Rosen

Research output: Contribution to journalArticle

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 Å 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 β-strands flanked by four α-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 c ntact points of the two proteins and forms the basis for future experiments.

Original languageEnglish (US)
Pages (from-to)5206-5212
Number of pages7
JournalBiochemistry
Volume49
Issue number25
DOIs
StatePublished - Jun 29 2010

ASJC Scopus subject areas

  • Biochemistry

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