PROSITE documentation PDOC51353Arsenate reductase arsC family profile
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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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Carlin A. Shi W. Dey S. Rosen B.P. |
| Title | The ars operon of Escherichia coli confers arsenical and antimonial resistance. | |
| Source | J. Bacteriol. 177:981-986(1995). | |
| PubMed ID | 7860609 |
| 2 | Authors | Liu J. Rosen B.P. |
| Title | Ligand interactions of the ArsC arsenate reductase. | |
| Source | J. Biol. Chem. 272:21084-21089(1997). | |
| PubMed ID | 9261111 |
| 3 | Authors | Zuber P. |
| Title | Spx-RNA polymerase interaction and global transcriptional control during oxidative stress. | |
| Source | J. Bacteriol. 186:1911-1918(2004). | |
| PubMed ID | 15028674 |
| 4 | Authors | Martin P. DeMel S. Shi J. Gladysheva T. Gatti D.L. Rosen B.P. Edwards B.F. |
| Title | Insights into the structure, solvation, and mechanism of ArsC arsenate reductase, a novel arsenic detoxification enzyme. | |
| Source | Structure 9:1071-1081(2001). | |
| PubMed ID | 11709171 |
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