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Resonance assignments and secondary structure prediction of the As(III) metallochaperone ArsD in solution.

ABSTRACT: ArsD is a metallochaperone that delivers As(III) to the ArsA ATPase, the catalytic subunit of the ArsAB pump encoded by the arsRDABC operon of Escherichia coli plasmid R773. Conserved ArsD cysteine residues (Cys(12), Cys(13) and Cys(18)) construct the As(III) binding site of the protein, however a global structural understanding of this arsenic binding remains unclear. We have obtained NMR assignments for ArsD as a starting point for probing structural changes on the protein that occur in response to metalloid binding and upon formation of a complex with ArsA. The predicted solution structure of ArsD is in agreement with recently published crystallographic structural results.

SUBMITTER: Ye J

PROVIDER: S-EPMC3364515 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature

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Resonance assignments and secondary structure prediction of the As(III) metallochaperone ArsD in solution.

Ye Jun J He Yanan Y Skalicky Jack J Rosen Barry P BP Stemmler Timothy L TL

Biomolecular NMR assignments 20101110 1

ArsD is a metallochaperone that delivers As(III) to the ArsA ATPase, the catalytic subunit of the ArsAB pump encoded by the arsRDABC operon of Escherichia coli plasmid R773. Conserved ArsD cysteine residues (Cys(12), Cys(13) and Cys(18)) construct the As(III) binding site of the protein, however a global structural understanding of this arsenic binding remains unclear. We have obtained NMR assignments for ArsD as a starting point for probing structural changes on the protein that occur in respon ...[more]

PMID: 21063813

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The ArsD As(III) metallochaperone.

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