ArsD residues Cys12, Cys13, and Cys18 form an As(III)-binding site required for arsenic metallochaperone activity.

@article{Lin2007ArsDRC,
  title={ArsD residues Cys12, Cys13, and Cys18 form an As(III)-binding site required for arsenic metallochaperone activity.},
  author={Y Lin and Jian-bo Yang and Barry P. Rosen},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 23},
  pages={16783-91}
}
The ArsA ATPase is the catalytic subunit of the ArsAB pump encoded by the arsRDABC operon of Escherichia coli plasmid R773. ArsD is a metallochaperone that delivers As(III) to ArsA, increasing its affinity for As(III), thus conferring resistance to environmental concentrations of arsenic. R773 ArsD is a homodimer with three vicinal cysteine pairs, Cys(12)-Cys(13), Cys(112)-Cys(113), and Cys(119)-Cys(120), in each subunit. Each vicinal pair binds As(III) or Sb(III). Alignment of the primary… CONTINUE READING