Interaction of ATP binding sites in the ArsA ATPase, the catalytic subunit of the Ars pump.

@article{Li1996InteractionOA,
  title={Interaction of ATP binding sites in the ArsA ATPase, the catalytic subunit of the Ars pump.},
  author={Jing Li and S Liu and Barry P. Rosen},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 41},
  pages={25247-52}
}
The ArsA ATPase is the catalytic subunit of the Ars pump that catalyzes arsenical extrusion in Escherichia coli, thus providing resistance. The active form of ArsA is a homodimer with four nucleotide binding sites, two from each monomer. The codons for Gly-15 in the N-terminal consensus nucleotide binding sequence and Gly-334 in the C-terminal sequence were… CONTINUE READING