Tryptophan fluorescence reports nucleotide-induced conformational changes in a domain of the ArsA ATPase.

@article{Zhou1997TryptophanFR,
  title={Tryptophan fluorescence reports nucleotide-induced conformational changes in a domain of the ArsA ATPase.},
  author={Tongqing Zhou and Barry P. Rosen},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 32},
  pages={19731-7}
}
The ars operon of plasmid R773 encodes an ATP-dependent extrusion pump for arsenite and antimonite in Escherichia coli. The ArsA ATPase is the catalytic subunit of the pump protein, with two nucleotide binding consensus sequences, one in the NH2-terminal half and one in the COOH-terminal half of the protein. A 12-residue consensus sequence (DTAPTGHTIRLL) has been identified in ArsA homologs from eubacteria, archebacteria, fungi, plants, and animals. ArsA enzymes were constructed containing… CONTINUE READING