Arsenate reductase
From Proteopedia
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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=''> | <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=''> | ||
| + | == Function == | ||
| - | '''Arsenate reductase''' (AsR) catalyzes the conversion of arsenate (As) and glutaredoxin to arsenite and glutaredoxin disulfide. AsR is part of the arsenic detoxification pathway. | + | '''Arsenate reductase''' (AsR) catalyzes the conversion of arsenate (As V) and glutaredoxin to arsenite (As III) and glutaredoxin disulfide. |
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| + | == Relevance == | ||
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| + | AsR is part of the arsenic detoxification pathway. | ||
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| + | == Structural highlights == | ||
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| + | The AsR active site contains a catalytic Sys residue which forms a covalent thiolate-As V intermediate. | ||
</StructureSection> | </StructureSection> | ||
Revision as of 11:48, 4 November 2015
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3D structures of arsenate reducatse
Updated on 04-November-2015
