Ars operon

Anion-transporting ATPase
Identifiers
SymbolArsA_ATPase
PfamPF02374
Pfam clanCL0023
SCOP21f48 / SCOPe / SUPFAM
TCDB3.A.4
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
ArsB
Identifiers
SymbolArsB
PfamPF02040
Pfam clanCL0182
InterProIPR000802
TCDB3.A.4
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
ArsC
yffb (pa3664) protein
Identifiers
SymbolArsC
PfamPF03960
Pfam clanCL0172
InterProIPR006660
SCOP21i9d / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
ArsD
Identifiers
SymbolArsD
PfamPF06953
Pfam clanCL0172
InterProIPR010712
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
ArsR
Identifiers
SymbolArsR
PfamPF09824
Pfam clanCL0123
InterProIPR018334
SCOP2a.4.5.5 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

In molecular biology, the ars operon is an operon found in several bacterial taxon. It is required for the detoxification of arsenate, arsenite, and antimonite.[1] This system transports arsenite and antimonite out of the cell. The pump is composed of two polypeptides, the products of the arsA and arsB genes. This two-subunit enzyme produces resistance to arsenite and antimonite. Arsenate, however, must first be reduced to arsenite before it is extruded. A third gene, arsC, expands the substrate specificity to allow for arsenate pumping and resistance. ArsC is an approximately 150-residue arsenate reductase that uses reduced glutathione (GSH) to convert arsenate to arsenite with a redox active cysteine residue in the active site. ArsC forms an active quaternary complex with GSH, arsenate, and glutaredoxin 1 (Grx1). The three ligands must be present simultaneously for reduction to occur.[2]

  1. ^ Carlin A, Shi W, Dey S, Rosen BP (February 1995). "The ars operon of Escherichia coli confers arsenical and antimonial resistance". J. Bacteriol. 177 (4): 981–6. doi:10.1128/jb.177.4.981-986.1995. PMC 176692. PMID 7860609.
  2. ^ Liu J, Rosen BP (August 1997). "Ligand interactions of the ArsC arsenate reductase". J. Biol. Chem. 272 (34): 21084–9. doi:10.1074/jbc.272.34.21084. PMID 9261111.