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Literature summary for 7.3.2.7 extracted from

  • Ajees, A.A.; Yang, J.; Rosen, B.P.
    The ArsD As(III) metallochaperone (2011), Biometals, 24, 391-399.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
ArsD ArsD is an arsenic chaperone for ArsA. ArsD transfers As(III) to ArsA and increases the affinity of ArsA for As(III). Cys12, Cys13 and Cys18 in ArsD form a three sulfur-coordinated As(III) binding site that is essential for metallochaperone activity, Interaction between ArsD and ArsA, ArsD function, overview Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + antimonite/in Escherichia coli
-
ADP + phosphate + antimonite/out
-
?
ATP + H2O + arsenite/in Escherichia coli
-
ADP + phosphate + arsenite/out
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
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ArsAB pump is encoded in arsRDABC operon on plasmid R773
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + antimonite/in
-
Escherichia coli ADP + phosphate + antimonite/out
-
?
ATP + H2O + arsenite/in
-
Escherichia coli ADP + phosphate + arsenite/out
-
?

General Information

General Information Comment Organism
physiological function ArsA is an ATPase that is the catalytic subunit of the ArsAB As(III) extrusion pump, and ArsD is an arsenic chaperone for ArsA. ArsD transfers As(III) to ArsA and increases the affinity of ArsA for As(III), allowing resistance to environmental concentrations of arsenic. ATP hydrolysis by ArsA is required for transfer of As(III) from ArsD to ArsA, suggesting that transfer occurs with a conformation of ArsA that transiently forms during the catalytic cycle. Docking of ArsD with ArsA, modeling and mechanism, detailed overview. Cysteine-rich metalloid binding sites of ArsD and ArsA come close to each other during interaction, ArsD interacts with nucleotide-bound form. The interface with ArsA involves one surface of alpha1 helix and metalloid binding site of ArsD. ArsB is a As(OH)3/H+ antiporter that extrudes As(III), conferring resistance Escherichia coli