2d2h
From Proteopedia
(New page: 200px<br /><applet load="2d2h" size="350" color="white" frame="true" align="right" spinBox="true" caption="2d2h, resolution 1.80Å" /> '''OpdA from Agrobacter...) |
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==Overview== | ==Overview== | ||
| - | A detailed understanding of the catalytic mechanism of enzymes is an | + | 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 Structure== | ==About this Structure== | ||
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[[Category: Aryldialkylphosphatase]] | [[Category: Aryldialkylphosphatase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Carr, P | + | [[Category: Carr, P D.]] |
[[Category: Jackson, C.]] | [[Category: Jackson, C.]] | ||
| - | [[Category: Kim, H | + | [[Category: Kim, H K.]] |
| - | [[Category: Liu, J | + | [[Category: Liu, J W.]] |
| - | [[Category: Ollis, D | + | [[Category: Ollis, D L.]] |
[[Category: CO]] | [[Category: CO]] | ||
[[Category: CO2]] | [[Category: CO2]] | ||
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[[Category: phosphotriesterase]] | [[Category: phosphotriesterase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:54:41 2008'' |
Revision as of 14:54, 21 February 2008
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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.
About 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.
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
Page seeded by OCA on Thu Feb 21 16:54:41 2008
Categories: Agrobacterium tumefaciens | Aryldialkylphosphatase | Single protein | Carr, P D. | Jackson, C. | Kim, H K. | Liu, J W. | Ollis, D L. | CO | CO2 | TZZ | Metalloenzyme | Opda | Phosphotriesterase
