EC Number   |
Subunits |
Reference |
|---|
   7.3.2.7 | ? |
x * 63000, ArsA, containing two ABC domains, structure model, overview |
695985 |
| 7.3.2.7 | ? |
x * 63000, recombinant ArsA, SDS-PAGE |
-, 718867 |
| 7.3.2.7 | heterodimer |
the enzyme is composed of ATPase subunit ArsA and arsenic-efflux pump ArsB |
699223 |
| 7.3.2.7 | More |
ArsA ATPase, the catalytic subunit of the pump, has two homologous halves, A1 and A2, and at the interface of these two halves are two nucleotide-binding domains and a metalloid-binding domain, Cys113 and Cys422 form a high-affinity metalloid binding site. There is only a single high-affinity metalloid binding site in ArsA, and second that Cys172 controls the affinity of this site for metalloid and hence the efficiency of metalloactivation of the ArsAB efflux pump |
689052 |
| 7.3.2.7 | More |
ArsA is composed of two homologous halves A1 and A2, each containing a nucleotide binding domain, and a single metalloid binding or activation domain is located at the interface of the two halves of the protein. The metalloid binding domain is connected to the two nucleotide binding domains through two DTAPTGH sequences, one in A1 and the other in A2. The DTAPTGH sequences are proposed to be involved in information communication between the metal and catalytic sites |
696278 |
| 7.3.2.7 | More |
ArsA is the catalytic subunit of the ArsAB arsenite (As(III)) translocating ATPase, ArsA exhibits ATpase activity |
719132 |
| 7.3.2.7 | More |
ArsA structure analysis and comparison, PDB entry 1F48, overview |
-, 718867 |
| 7.3.2.7 | More |
subunit ArsA exhibuts ATPase activity and subunit ArsB is a 12 alpha-helix transmembrane spanning pump extruding As(III) and Sb(III) |
719612 |
| 7.3.2.7 | More |
the ArsA is a 63000 Da protein, Ars B is a 45500 Da protein, ArsC is a 16000 Da, protein. ArsB, with 12 membrane-spanning segments forms the channel part and ArsA, occuring in pairs peripherally to the membrane |
210288 |
| 7.3.2.7 | More |
the ArsA protein is a membrane associated ATPase, energizing the arsenite efflux pump by ATP hydrolysis, ArsA is attached to the ArsB inner-membrane protein. The ArsB protein can function alone as a chemiosmotic, membrane-potential driven arsenite-efflux transporter or together with ArsA as an ATP-driven primary membrane pump. ArsC reduces loss toxic arsenate to more toxic arsenite, the substrate for the ArsB transport protein |
210279 |
