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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=''>
<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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== 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''' (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

Structure of arsenate reductase complex with arsenate, thiarsahydroxy-cysteine, sulfate and Cs+ ion (dark purple) (PDB entry 1j9b)

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3D structures of arsenate reducatse

Updated on 04-November-2015

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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