Arsenate reductase: Difference between revisions

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</StructureSection>
</StructureSection>


== 3D structures of arsenate reductase==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
* Arsenate reductase
**[[1jf8]], [[1ljl]] – SaAsR – ''Staphylococcus aureus'' <BR />
**[[1jfv]], [[1lk0]], [[1rxi]], [[2cd7]], [[2fxi]] – SaAsR (mutant) <BR />
**[[1jl3]] – BsAsR – ''Bacillus subtilis'' <BR />
**[[1z2d]], [[1z2e]] – BsAsR - NMR <BR />
**[[1i9d]] – EcAsR – ''Escherichia coli'' <BR />
**[[1s3c]], [[1s3d]], [[1sd8]], [[1sd9]], [[1sk2]] – EcAsR (mutant) <BR />
**[[2l17]], [[2l18]], [[2myn]], [[2myp]] – SyAsR – ''Synechocystis'' - NMR<BR />
**[[2l19]], [[2myt]], [[2myu]] – SyAsR (mutant) - NMR<BR />
**[[1y1l]] – AsR – ''Archaeoglobus fulgidus''<br />
**[[3f0i]] – AsR – ''Vibrio cholerae''<br />
**[[2kok]], [[2mu0]] – AsR – ''Brucella abortus''<br />
**[[3rh0]], [[3t38]] – AsR – ''Corynebacterium glutamicum''<br />
*Arsenate reductase complexes
**[[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]]

Revision as of 11:37, 20 March 2019


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]

3D structures of arsenate reductase

Arsenate reductase 3D structures


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

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

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Michal Harel, Alexander Berchansky
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