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The 1.4 A crystal structure of the ArsD arsenic metallochaperone provides insights into its interaction with the ArsA ATPase

Ye, J.; Ajees, A.A.; Yang, J.; Rosen, B.P.; Biochemistry 49, 5206-5212 (2010)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
7.3.2.7
ArsD
arsenic metallochaperone ArsD delivers As(III) to the ArsA ATPase, the catalytic subunit of the ArsAB pump. ArsD binds one arsenic per monomer coordinated with the three sulfur atoms of Cys12, Cys13 and Cys18, modeling of ArsD with and without bound As(III), overview. For analysis of metallo chaperone activity a recombinant truncated form, ArsD109, is used
Saccharomyces cerevisiae
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 + antimonite/in
Saccharomyces cerevisiae
-
ADP + phosphate + antimonite/out
-
-
-
7.3.2.7
ATP + H2O + arsenite/in
Saccharomyces cerevisiae
-
ADP + phosphate + arsenite/out
-
-
-
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
7.3.2.7
Saccharomyces cerevisiae
-
-
-
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 + antimonite/in
-
718876
Saccharomyces cerevisiae
ADP + phosphate + antimonite/out
-
-
-
-
7.3.2.7
ATP + H2O + arsenite/in
-
718876
Saccharomyces cerevisiae
ADP + phosphate + arsenite/out
-
-
-
-
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
7.3.2.7
ArsD
arsenic metallochaperone ArsD delivers As(III) to the ArsA ATPase, the catalytic subunit of the ArsAB pump. ArsD binds one arsenic per monomer coordinated with the three sulfur atoms of Cys12, Cys13 and Cys18, modeling of ArsD with and without bound As(III), overview. For analysis of metallo chaperone activity a recombinant truncated form, ArsD109, is used
Saccharomyces cerevisiae
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 + antimonite/in
Saccharomyces cerevisiae
-
ADP + phosphate + antimonite/out
-
-
-
7.3.2.7
ATP + H2O + arsenite/in
Saccharomyces cerevisiae
-
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 + antimonite/in
-
718876
Saccharomyces cerevisiae
ADP + phosphate + antimonite/out
-
-
-
-
7.3.2.7
ATP + H2O + arsenite/in
-
718876
Saccharomyces cerevisiae
ADP + phosphate + arsenite/out
-
-
-
-
General Information
EC Number
General Information
Commentary
Organism
7.3.2.7
additional information
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
Saccharomyces cerevisiae
General Information (protein specific)
EC Number
General Information
Commentary
Organism
7.3.2.7
additional information
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
Saccharomyces cerevisiae