FunctionArsenate reductase (AsR) catalyzes the conversion of arsenate (As V) and glutaredoxin to arsenite (As III) and glutaredoxin disulfide.[1]
RelevanceAsR is part of the arsenic detoxification pathway.
Structural highlightsThe AsR active site contains a . (PDB entry 1j9b).[2]
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3D structures of arsenate reductase3D structures of arsenate reductase
Updated on 08-December-2015
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- Arsenate reductase
- 1jf8, 1ljl – SaAsR – Staphylococcus aureus
- 1jfv, 1lk0, 1rxi, 2cd7, 2fxi – SaAsR (mutant)
- 1jl3 – BsAsR – Bacillus subtilis
- 1z2d, 1z2e – BsAsR - NMR
- 1i9d – EcAsR – Escherichia coli
- 1s3c, 1s3d, 1sd8, 1sd9, 1sk2 – EcAsR (mutant)
- 2l17, 2l18 – SyAsR – Synechocystis - NMR
- 2l19 – SyAsR (mutant) - NMR
- 1y1l – AsR – Archaeoglobus fulgidus
- 3f0i – AsR – Vibrio cholerae
- 3rh0, 3t38 – AsR – Corynebacterium glutamicum
- Arsenate reductase complexes
- 1jzw – EcAsR + arsonocysteine
- 1sk1 – EcAsR (mutant) + arsonocysteine
- 1sjz, 1sk0 – EcAsR (mutant) + arsonocysteine + AsO3
- 1j9b – EcAsR + AsO3 + thiarsahydroxy-cysteine
- 1lju – SaAsR (mutant) + arsonocysteine
- 1rxe – SaAsR (mutant) + mercapto-nitrobenzoate
- 2ipa – BsAsR (mutant) + thioredoxin (mutant)
ReferencesReferences
- ↑ Holmgren A, Aslund F. Glutaredoxin. Methods Enzymol. 1995;252:283-92. PMID:7476363
- ↑ Martin P, DeMel S, Shi J, Gladysheva T, Gatti DL, Rosen BP, Edwards BF. Insights into the structure, solvation, and mechanism of ArsC arsenate reductase, a novel arsenic detoxification enzyme. Structure. 2001 Nov;9(11):1071-81. PMID:11709171
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