Arsenate reductase: Difference between revisions

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**[[1i9d]] – EcAsR – ''Escherichia coli'' <BR />
**[[1i9d]] – EcAsR – ''Escherichia coli'' <BR />
**[[1s3c]], [[1s3d]], [[1sd8]], [[1sd9]], [[1sk2]] – EcAsR (mutant) <BR />
**[[1s3c]], [[1s3d]], [[1sd8]], [[1sd9]], [[1sk2]] – EcAsR (mutant) <BR />
**[[2l17]], [[2l18], [[2myn]], [[2myp]] – SyAsR – ''Synechocystis'' - NMR<BR />
**[[2l17]], [[2l18]], [[2myn]], [[2myp]] – SyAsR – ''Synechocystis'' - NMR<BR />
**[[2l19]], [[2myt]], [[2myu]] – SyAsR (mutant) - NMR<BR />
**[[2l19]], [[2myt]], [[2myu]] – SyAsR (mutant) - NMR<BR />
**[[1y1l]] – AsR – ''Archaeoglobus fulgidus''<br />
**[[1y1l]] – AsR – ''Archaeoglobus fulgidus''<br />

Revision as of 13:02, 9 March 2017


Function

Arsenate reductase (AsR) catalyzes the conversion of arsenate (As V) and glutaredoxin to arsenite (As III) and glutaredoxin disulfide.[1]

Relevance

AsR is part of the arsenic detoxification pathway.

Structural highlights

The AsR active site contains a . (PDB entry 1j9b).[2]

Structure of arsenate reductase complex with arsenate, thiarsahydroxy-cysteine, sulfate and Cs+ ion (dark purple) (PDB entry 1j9b)

Drag the structure with the mouse to rotate

3D structures of arsenate reductase3D structures of arsenate reductase

Updated on 09-March-2017

ReferencesReferences

  1. Holmgren A, Aslund F. Glutaredoxin. Methods Enzymol. 1995;252:283-92. PMID:7476363
  2. 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky