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Crystallization and preliminary X-ray analysis of the catalytic subunit of the ATP-dependent arsenite pump encoded by the Escherichia coli plasmid R773

Zhou, T.; Rosen, B.P.; Gatti, D.L.; Acta Crystallogr. Sect. D 55, 921-924 (1999)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
Organism
7.3.2.7
catalytic subunit of the ATP-dependent arsenite pump is encoded by the Escherichia coli plasmid R773
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
detoxifying system
ADP + phosphate + arsenite/out
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
7.3.2.7
Escherichia coli
-
from plasmid R773
-
Purification (Commentary)
EC Number
Commentary
Organism
7.3.2.7
-
Escherichia coli
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
-
210279
Escherichia coli
ADP + phosphate + arsenite/out
-
210279
Escherichia coli
?
7.3.2.7
ATP + H2O + arsenite/in
detoxifying system
210279
Escherichia coli
ADP + phosphate + arsenite/out
-
-
-
?
7.3.2.7
additional information
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 converts the less toxic arsenate to more toxic arsenite, the substrate for the ArsB transport protein
210279
Escherichia coli
?
-
-
-
-
Subunits
EC Number
Subunits
Commentary
Organism
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
Escherichia coli
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
7.3.2.7
catalytic subunit of the ATP-dependent arsenite pump is encoded by the Escherichia coli plasmid R773
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
detoxifying system
ADP + phosphate + arsenite/out
-
-
?
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
7.3.2.7
-
Escherichia coli
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
-
210279
Escherichia coli
ADP + phosphate + arsenite/out
-
210279
Escherichia coli
?
7.3.2.7
ATP + H2O + arsenite/in
detoxifying system
210279
Escherichia coli
ADP + phosphate + arsenite/out
-
-
-
?
7.3.2.7
additional information
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 converts the less toxic arsenate to more toxic arsenite, the substrate for the ArsB transport protein
210279
Escherichia coli
?
-
-
-
-
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
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
Escherichia coli