Article
Cys-113 and Cys-422 form a high affinity metalloid binding site in the ArsA ATPase.
The Journal of biological chemistry - 14 Apr 2006
Ruan Xiang, Bhattacharjee Hiranmoy, Rosen Barry P
Abstract excerpt
The arsRDABC operon of Escherichia coli plasmid R773 encodes the ArsAB extrusion pump for the trivalent metalloids As(III) and Sb(III). ArsA, the catalytic subunit has two homologous halves, A1 and A2. Each half has a consensus signal transduction domain that physically connects the nucleotide-binding domain to the metalloid-binding domain. The relation between metalloid binding by ArsA and transport through ArsB...
Topics
- Adenosine Triphosphatases
- Adenosine Triphosphate
- Antimony Potassium Tartrate
- Arsenites
- Binding Sites
- Catalysis
- Catalytic Domain
- Codon
- Cysteine
- Dose-Response Relationship, Drug
- Escherichia coli
- Escherichia coli Proteins
- Hydrolysis
- Ion Pumps