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Characterization of the metalloactivation domain of an arsenite/antimonite resistance pump

Ruan, X.; Bhattacharjee, H.; Rosen, B.P.; Mol. Microbiol. 67, 392-402 (2008)

Data extracted from this reference:

Engineering
EC Number
Amino acid exchange
Commentary
Organism
7.3.2.7
C113A/C422A
site-directed mutagenesis, the mutant lacks As(III) activation activity compared to the wild-type enzyme
Escherichia coli
7.3.2.7
C172A
site-directed mutagenesis, an ArsA mutant, the mutant shows reduced affinity for Sb(III) compared to the wild-type enzyme
Escherichia coli
7.3.2.7
C172A/H453A
site-directed mutagenesis, the ArsA double mutant exhibits significantly decreased affinity for Sb(III)
Escherichia coli
7.3.2.7
H148A/S420A
site-directed mutagenesis, the mutant exhibits a half-maximal stimulation similar to that of the wild-type enzyme
Escherichia coli
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
7.3.2.7
ATP + H2O + arsenite/in
Escherichia coli
the ArsAB extrusion pump confers resistance to the toxic trivalent metalloids arsenite [As(III)] and antimonite [Sb(III)], overview
ADP + phosphate + arsenite/out
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
7.3.2.7
Escherichia coli
P08690
the enzyme is encoded by the ars operon of plasmid R773
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
7.3.2.7
ATP + H2O + arsenite/in
the ArsAB extrusion pump confers resistance to the toxic trivalent metalloids arsenite [As(III)] and antimonite [Sb(III)], overview
689052
Escherichia coli
ADP + phosphate + arsenite/out
-
-
-
?
7.3.2.7
ATP + H2O + arsenite/in
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. Two other metalloid atoms are bound, one liganded to Cys172 and His453, and the other liganded to His148 and Ser420, but 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, metalloid binding site MBS structure and mechanism, overview
689052
Escherichia coli
ADP + phosphate + arsenite/out
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
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
Escherichia coli
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
7.3.2.7
C113A/C422A
site-directed mutagenesis, the mutant lacks As(III) activation activity compared to the wild-type enzyme
Escherichia coli
7.3.2.7
C172A
site-directed mutagenesis, an ArsA mutant, the mutant shows reduced affinity for Sb(III) compared to the wild-type enzyme
Escherichia coli
7.3.2.7
C172A/H453A
site-directed mutagenesis, the ArsA double mutant exhibits significantly decreased affinity for Sb(III)
Escherichia coli
7.3.2.7
H148A/S420A
site-directed mutagenesis, the mutant exhibits a half-maximal stimulation similar to that of the wild-type enzyme
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
7.3.2.7
ATP + H2O + arsenite/in
Escherichia coli
the ArsAB extrusion pump confers resistance to the toxic trivalent metalloids arsenite [As(III)] and antimonite [Sb(III)], overview
ADP + phosphate + arsenite/out
-
-
?
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
7.3.2.7
ATP + H2O + arsenite/in
the ArsAB extrusion pump confers resistance to the toxic trivalent metalloids arsenite [As(III)] and antimonite [Sb(III)], overview
689052
Escherichia coli
ADP + phosphate + arsenite/out
-
-
-
?
7.3.2.7
ATP + H2O + arsenite/in
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. Two other metalloid atoms are bound, one liganded to Cys172 and His453, and the other liganded to His148 and Ser420, but 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, metalloid binding site MBS structure and mechanism, overview
689052
Escherichia coli
ADP + phosphate + arsenite/out
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
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
Escherichia coli