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PROSITE documentation PDOC51353 [for PROSITE entry PS51353]

Arsenate reductase arsC family profile





Description

Several bacterial taxon have a chromosomal resistance system, encoded by the ars operon, for the detoxification of arsenate, arsenite, and antimonite [1]. This system transports arsenite and antimonite out of the cell. Arsenate, however, must first be reduced to arsenite before it is extruded. ArsC is an ~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].

The arsC family also comprises the Spx proteins which are GRAM-positive bacterial transcription factors that regulate the transcription of multiple genes in response to disulfide stress [3].

The arsC protein structure has been solved (see <PDB:1I9D>) [4]. It belongs to the thioredoxin superfamily fold which is defined by a β-sheet core surrounded by α-helices. The active cysteine residue of ArsC is located in the loop between the first β-strand and the first helix, which is also conserved in the Spx protein and its homologs.

The profile we developed covers the whole arsC conserved region.

Last update:

December 2007 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

ARSC, PS51353; ArsC family profile  (MATRIX)


References

1AuthorsCarlin A. Shi W. Dey S. Rosen B.P.
TitleThe ars operon of Escherichia coli confers arsenical and antimonial resistance.
SourceJ. Bacteriol. 177:981-986(1995).
PubMed ID7860609

2AuthorsLiu J. Rosen B.P.
TitleLigand interactions of the ArsC arsenate reductase.
SourceJ. Biol. Chem. 272:21084-21089(1997).
PubMed ID9261111

3AuthorsZuber P.
TitleSpx-RNA polymerase interaction and global transcriptional control during oxidative stress.
SourceJ. Bacteriol. 186:1911-1918(2004).
PubMed ID15028674

4AuthorsMartin P. DeMel S. Shi J. Gladysheva T. Gatti D.L. Rosen B.P. Edwards B.F.
TitleInsights into the structure, solvation, and mechanism of ArsC arsenate reductase, a novel arsenic detoxification enzyme.
SourceStructure 9:1071-1081(2001).
PubMed ID11709171



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