2d2h
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OpdA from Agrobacterium radiobacter with bound inhibitor trimethyl phosphate at 1.8 A resolution
OverviewOverview
A detailed understanding of the catalytic mechanism of enzymes is an, important step toward improving their activity for use in biotechnology., In this paper, crystal soaking experiments and X-ray crystallography were, used to analyse the mechanism of the Agrobacterium radiobacter, phosphotriesterase, OpdA, an enzyme capable of detoxifying a broad range, of organophosphate pesticides. The structures of OpdA complexed with, ethylene glycol and the product of dimethoate hydrolysis, dimethyl, thiophosphate, provide new details of the catalytic mechanism. These, structures suggest that the attacking nucleophile is a terminally bound, hydroxide, consistent with the catalytic mechanism of other binuclear, metallophosphoesterases. In addition, a crystal structure with the, potential substrate trimethyl phosphate bound non-productively, demonstrates the importance of the active site cavity in orienting the, substrate into an approximation of the transition state.
About this StructureAbout this Structure
2D2H is a Single protein structure of sequence from Agrobacterium tumefaciens with , and as ligands. Active as Aryldialkylphosphatase, with EC number 3.1.8.1 Full crystallographic information is available from OCA.
ReferenceReference
The structure of an enzyme-product complex reveals the critical role of a terminal hydroxide nucleophile in the bacterial phosphotriesterase mechanism., Jackson C, Kim HK, Carr PD, Liu JW, Ollis DL, Biochim Biophys Acta. 2005 Aug 31;1752(1):56-64. PMID:16054447
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