Arsenate reductase: Difference between revisions

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== 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> (PDB entry [[1j9b]]).<ref>PMID:11709171</ref>  
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>
</StructureSection>



Revision as of 13:32, 7 January 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]

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 07-January-2019

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