2d2h: Difference between revisions

Revision as of 22:55, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2d2h.png

Template:STRUCTURE 2d2h

OpdA from Agrobacterium radiobacter with bound inhibitor trimethyl phosphate at 1.8 A resolutionOpdA from Agrobacterium radiobacter with bound inhibitor trimethyl phosphate at 1.8 A resolution

Template:ABSTRACT PUBMED 16054447

About this StructureAbout this Structure

2D2H is a Single protein structure of sequence from Agrobacterium tumefaciens. 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

Page seeded by OCA on Sun Jul 27 22:55:43 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''OpdA from Agrobacterium radiobacter with bound inhibitor trimethyl phosphate at 1.8 A resolution'''
+===OpdA from Agrobacterium radiobacter with bound inhibitor trimethyl phosphate at 1.8 A resolution===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16054447}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_16054447}}
 ==About this Structure==
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 [[Category: Opda]]
 [[Category: Phosphotriesterase]]
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