2d2g

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{{Seed}}
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{{STRUCTURE_2d2g| PDB=2d2g | SCENE= }}
{{STRUCTURE_2d2g| PDB=2d2g | SCENE= }}
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'''OpdA from Agrobacterium radiobacter with bound product dimethylthiophosphate'''
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===OpdA from Agrobacterium radiobacter with bound product dimethylthiophosphate===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 16054447 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16054447}}
==About this Structure==
==About this Structure==
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[[Category: Opda]]
[[Category: Opda]]
[[Category: Phosphotriesterase]]
[[Category: Phosphotriesterase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:34:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:19:06 2008''

Revision as of 05:19, 29 July 2008

Image:2d2g.png

Template:STRUCTURE 2d2g

OpdA from Agrobacterium radiobacter with bound product dimethylthiophosphate

Template:ABSTRACT PUBMED 16054447

About this Structure

2D2G is a Single protein structure of sequence from Agrobacterium tumefaciens. Full crystallographic information is available from OCA.

Reference

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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