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Literature summary for 7.3.2.7 extracted from

  • Fu, H.; Ajees, A.; Rosen, B.; Bhattacharjee, H.
    Role of signature lysines in the deviant walker a motifs of the ArsA ATPase (2010), Biochemistry, 49, 356-364.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged wild-type and mutant enzymes Escherichia coli

Protein Variants

Protein Variants Comment Organism
K16Q site-directed mutagenesis, the mutant ArsA shows 70% of wild-type ATPase activity Escherichia coli
K335Q site-directed mutagenesis, the mutant ArsA is inactive. K335Q acquires a closed conformation during metalloid-stimulated catalysis that is different from the open conformation of the wild-type Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli
Sb3+ ArsA is activated by binding of Sb(III), and both wild-type and mutant K16Q ArsAs bind Sb(III) with a 1:1 stoichiometry Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
63000
-
x * 63000, recombinant ArsA, SDS-PAGE 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 + antimonite/in Escherichia coli JM109
-
ADP + phosphate + antimonite/out
-
?
ATP + H2O + arsenite/in Escherichia coli
-
ADP + phosphate + arsenite/out
-
?
ATP + H2O + arsenite/in Escherichia coli JM109
-
ADP + phosphate + arsenite/out
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
gene arsA
-
Escherichia coli JM109
-
gene arsA
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes by nickel affinity chromatography Escherichia coli

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 + antimonite/in
-
Escherichia coli JM109 ADP + phosphate + antimonite/out
-
?
ATP + H2O + arsenite/in
-
Escherichia coli ADP + phosphate + arsenite/out
-
?
ATP + H2O + arsenite/in
-
Escherichia coli JM109 ADP + phosphate + arsenite/out
-
?
additional information Lys16 is not critical for ATPase activity, while Lys335 is involved in intersubunit interaction and activation of ATPase activity in both halves of the protein Escherichia coli ?
-
?
additional information Lys16 is not critical for ATPase activity, while Lys335 is involved in intersubunit interaction and activation of ATPase activity in both halves of the protein Escherichia coli JM109 ?
-
?

Subunits

Subunits Comment Organism
? x * 63000, recombinant ArsA, SDS-PAGE Escherichia coli
More ArsA structure analysis and comparison, PDB entry 1F48, overview Escherichia coli

Synonyms

Synonyms Comment Organism
ArsA ATPase
-
Escherichia coli

General Information

General Information Comment Organism
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 Escherichia coli
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 Escherichia coli
additional information 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 Escherichia coli
physiological function the ArsAB pump in Escherichia coli, encoded by the ars operon of plasmid R773, confers resistance to arsenicals and antimonials. ArsA is the catalytic subunit of the pump that hydrolyzesATP in the presence of arsenite [As(III)] or antimonite [Sb(III)]. ATP hydrolysis is coupled to extrusion of As(III) or Sb(III) through ArsB, which serves both as a membrane anchor for ArsA and as the substrate-conducting pathway Escherichia coli