EC Number   |
General Information |
Reference |
|---|
   7.3.2.7 | evolution |
phylogenetic analysis of gene arsA and prokaryotic and eukaryotic ArsA homologues with detailed analysis of clustering in the superfamily, overview |
719612 |
| 7.3.2.7 | evolution |
the ArsA ATPase belongs to the P-loop GTPase subgroup within the GTPase superfamily of proteins, members of this subgroup have a deviant Walker A motif |
-, 718867 |
| 7.3.2.7 | malfunction |
mutations rendered the aquaglyceroporin channel more polar resulting in lower glycerol permeability and enhanced arsenite selectivity |
715567 |
| 7.3.2.7 | malfunction |
while Lys16 mutants show similar resistance phenotypes as the wild type, the Lys335 mutants are sensitive to higher concentrations of arsenite. The As(III)/Sb(III) binding affinity decreases in the order ArsA wild-type > K16Q > K335Q |
-, 718867 |
| 7.3.2.7 | more |
ARsA ATPase contains a deviant Walker A motif which has a signature lysine that is predicted to make intermonomer contact with the bound nucleotides and to play a role in ATP hydrolysis. ArsA has two signature lysines located at positions 16 and 335. Both wild-type and K16Q adopt a similar conformation during activated catalysis, whereas K335Q adopts a conformation that is resistant to trypsin cleavage |
-, 718867 |
| 7.3.2.7 | more |
ArsD is a metallochaperone that delivers trivalent metalloids [As(III) or Sb(III)] to the ArsA ATPase, the catalytic subunit of the ArsAB pump. ArsD residues Cys12, Cys13, and Cys18 are involved in the transfer of As(III) to ArsA. Transfer of As(III) from ArsD to ArsA occurs in the presence of MgATP, neither MgADP nor MgATP-gamma-S can replace MgATP. Transfer occurs with a conformation of ArsA that transiently forms during the catalytic cycle and not simply to the closed conformation that ArsA adopts when As(III) and MgATP are bound |
718868 |
| 7.3.2.7 | more |
for arsenite transport, metallated ArsD interacts with and transfers As(III) to ArsA during catalysis, when the ATPase cycles between open to closed conformations, structure and ArsD-ArsA interaction analysis, docking of ArsD and ArsA and modeling, overview |
718876 |
| 7.3.2.7 | more |
the Cys108 of AmArsA1 and Cys120 of AmArsA2 form part of the metalloid binding domain |
719496 |
| 7.3.2.7 | more |
the Strop634 channel domain has enhanced selectivity for arsenite and low glycerol permeability |
715567 |
| 7.3.2.7 | physiological function |
AmArsA1-AmArsA2 interaction is needed to form the functional ArsA ATPase. This novel AmArsA1-AmArsA2 complex may provide insight in how it participates with Acr3 in arsenite detoxification. ArsB transports antimonite, while Acr3 does not appear to do so |
719496 |
