Arsenate reductase
From Proteopedia
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== Function == | == Function == | ||
- | '''Arsenate reductase''' (AsR) catalyzes the conversion of arsenate (As V) and glutaredoxin to arsenite (As III) and glutaredoxin disulfide.<ref>PMID:7476363</ref> | + | '''Arsenate reductase''' or '''glutaredoxin arsenate reductase''' (AsR) catalyzes the conversion of arsenate (As V) and glutaredoxin to arsenite (As III) and glutaredoxin disulfide.<ref>PMID:7476363</ref> |
== Relevance == | == Relevance == | ||
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== Structural highlights == | == Structural highlights == | ||
- | The AsR active site contains a <scene name='54/547051/Cv/ | + | The AsR active site contains a <scene name='54/547051/Cv/5'>catalytic Cys residue which forms a covalent thiolate-As V intermediate</scene>. <scene name='54/547051/Cv/6'>Entire active site</scene> (PDB entry [[1j9b]]).<ref>PMID:11709171</ref> |
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== 3D structures of arsenate reductase== | == 3D structures of arsenate reductase== | ||
+ | [[Arsenate reductase 3D structures]] | ||
- | + | </StructureSection> | |
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- | **[[1jzw]] – EcAsR + arsonocysteine <BR /> | ||
- | **[[1sk1]] – EcAsR (mutant) + arsonocysteine <BR /> | ||
- | **[[1sjz]], [[1sk0]] – EcAsR (mutant) + arsonocysteine + AsO3<BR /> | ||
- | **[[1j9b]] – EcAsR + AsO3 + thiarsahydroxy-cysteine<BR /> | ||
- | **[[1lju]] – SaAsR (mutant) + arsonocysteine <BR /> | ||
- | **[[1rxe]] – SaAsR (mutant) + mercapto-nitrobenzoate <BR /> | ||
- | **[[2ipa]] – BsAsR (mutant) + thioredoxin (mutant)<BR /> | ||
- | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] |
Current revision
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References
- ↑ 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