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Biomol NMR Assign. 2011 Apr;5(1):109-12. doi: 10.1007/s12104-010-9279-9. Epub 2010 Nov 10.

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

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1
Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, MI 48201, USA.

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.

PMID:
21063813
PMCID:
PMC3364515
DOI:
10.1007/s12104-010-9279-9
[Indexed for MEDLINE]
Free PMC Article
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