2cd7
From Proteopedia
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STAPHYLOCOCCUS AUREUS PI258 ARSENATE REDUCTASE (ARSC) H62Q MUTANT
Overview
In the thioredoxin (Trx)-coupled arsenate reductase family, arsenate, reductase from Staphylococcus aureus plasmid pI258 (Sa_ArsC) and from, Bacillus subtilis (Bs_ArsC) are structurally related detoxification, enzymes. Catalysis of the reduction of arsenate to arsenite involves a, P-loop (Cys10Thr11Gly12Asn13Ser14Cys15Arg16) structural motif and a, disulphide cascade between three conserved cysteine residues (Cys10, Cys82, and Cys89). For its activity, Sa_ArsC benefits from the binding of, tetrahedral oxyanions in the P-loop active site and from the binding of, potassium in a specific cation-binding site. In contrast, the steady-state, kinetic parameters of Bs_ArsC are not affected by sulphate or potassium., The commonly occurring mutation of a histidine (H62), located about 6 A, from the ... [(full description)]
About this Structure
2CD7 is a [Single protein] structure of sequence from [Staphylococcus aureus] with NA as [ligand]. Active as [Transferred entry: 1.20.4.1], with EC number [1.97.1.5]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Interplay between ion binding and catalysis in the thioredoxin-coupled arsenate reductase family., Roos G, Buts L, Van Belle K, Brosens E, Geerlings P, Loris R, Wyns L, Messens J, J Mol Biol. 2006 Jul 21;360(4):826-38. Epub 2006 Jun 6. PMID:16797027
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