Resonance assignments and secondary structure prediction of the As(III) metallochaperone ArsD in solution.
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.
Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, MI 48201, USA.
Jun
J
Ye
Yanan
Y
He
Jack
J
Skalicky
Barry P
BP
Rosen
Timothy L
TL
Stemmler
D000595:Amino Acid Sequence; D001151:Arsenic / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D056511:Metallochaperones / Q000737:chemistry*; D018832:Molecular Chaperones / Q000737:chemistry*; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D012996:Solutions
C558793:ArsD protein, E coli; D029968:Escherichia coli Proteins; D056511:Metallochaperones; D018832:Molecular Chaperones; D012996:Solutions; D001151:Arsenic