Arsenate reductase

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<StructureSection load='1j9b' size='350' side='right' caption='Structure of arsenate reductase complex with arsenate, thiarsahydroxy-cysteine, sulfate and Cs+ ion (dark purple) (PDB entry [[1j9b]])' scene=''>
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<StructureSection load='1j9b' size='350' side='right' caption='Structure of arsenate reductase complex with arsenate, thiarsahydroxy-cysteine, sulfate and Cs+ ion (dark purple) (PDB entry [[1j9b]])' scene='54/547051/Cv/1'>
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== Function ==
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'''Arsenate reductase''' (AsR) catalyzes the conversion of arsenate (As) and glutaredoxin to arsenite and glutaredoxin disulfide. AsR is part of the arsenic detoxification pathway.
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'''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>
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== 3D structures of arsenate reducatse==
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== Relevance ==
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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AsR is part of the arsenic detoxification pathway.
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{{#tree:id=OrganizedByTopic|openlevels=0|
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* Arsenate reductase
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== Structural highlights ==
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**[[1jf8]], [[1ljl]] – SaAsR – ''Staphylococcus aureus'' <BR />
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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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**[[1jfv]], [[1lk0]], [[1rxi]], [[2cd7]], [[2fxi]] – SaAsR (mutant) <BR />
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**[[1jl3]] – BsAsR – ''Bacillus subtilis'' <BR />
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**[[1z2d]], [[1z2e]] – BsAsR - NMR <BR />
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**[[1i9d]] – EcAsR – ''Escherichia coli'' <BR />
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**[[1s3c]], [[1s3d]], [[1sd8]], [[1sd9]], [[1sk2]] – EcAsR (mutant) <BR />
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**[[2l17]], [[2l18]] – SyAsR – ''Synechocystis'' - NMR<BR />
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**[[2l19]] – SyAsR (mutant) - NMR<BR />
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**[[1y1l]] – AsR – ''Archaeoglobus fulgidus''<br />
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**[[3f0i]] – AsR – ''Vibrio cholerae''<br />
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**[[3rh0]], [[3t38]] – AsR – ''Corynebacterium glutamicum''<br />
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*Arsenate reductase complexes
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== 3D structures of arsenate reductase==
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[[Arsenate reductase 3D structures]]
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**[[1jzw]] – EcAsR + arsonocysteine <BR />
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</StructureSection>
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**[[1sk1]] – EcAsR (mutant) + arsonocysteine <BR />
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**[[1sjz]], [[1sk0]] – EcAsR (mutant) + arsonocysteine + AsO3<BR />
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== References ==
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**[[1j9b]] – EcAsR + AsO3 + thiarsahydroxy-cysteine<BR />
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<references/>
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**[[1lju]] – SaAsR (mutant) + arsonocysteine <BR />
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**[[1rxe]] – SaAsR (mutant) + mercapto-nitrobenzoate <BR />
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**[[2ipa]] – BsAsR (mutant) + thioredoxin (mutant)<BR />
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}}
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[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

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

References

  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?)

Michal Harel, Alexander Berchansky

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