Arsenate reductase: Difference between revisions

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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.   
'''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 ==
Line 11: Line 11:
== Structural highlights ==
== Structural highlights ==


The AsR active site contains a <scene name='54/547051/Cv/4'>catalytic Cys residue which forms a covalent thiolate-As V intermediate</scene>. <scene name='54/547051/Cv/3'>Entire active site</scene>.  
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>  
</StructureSection>


== 3D structures of arsenate reducatse==
== 3D structures of arsenate reductase==
[[Arsenate reductase 3D structures]]


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
</StructureSection>
{{#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]] – SyAsR – ''Synechocystis'' - NMR<BR />
**[[2l19]] – SyAsR (mutant) - NMR<BR />
**[[1y1l]] – AsR – ''Archaeoglobus fulgidus''<br />
**[[3f0i]] – AsR – ''Vibrio cholerae''<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/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 12:12, 23 February 2021


Function

Arsenate reductase or glutaredoxin 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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