2d2h
From Proteopedia
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|PDB= 2d2h |SIZE=350|CAPTION= <scene name='initialview01'>2d2h</scene>, resolution 1.80Å | |PDB= 2d2h |SIZE=350|CAPTION= <scene name='initialview01'>2d2h</scene>, resolution 1.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=CO2:CARBON+DIOXIDE'>CO2</scene> | + | |LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=CO2:CARBON+DIOXIDE'>CO2</scene>, <scene name='pdbligand=TZZ:TRIMETHYL+PHOSPHATE'>TZZ</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Aryldialkylphosphatase Aryldialkylphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.8.1 3.1.8.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Aryldialkylphosphatase Aryldialkylphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.8.1 3.1.8.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2d2g|2D2G]], [[2d2j|2D2J]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d2h OCA], [http://www.ebi.ac.uk/pdbsum/2d2h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2d2h RCSB]</span> | ||
}} | }} | ||
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[[Category: Liu, J W.]] | [[Category: Liu, J W.]] | ||
[[Category: Ollis, D L.]] | [[Category: Ollis, D L.]] | ||
| - | [[Category: CO]] | ||
| - | [[Category: CO2]] | ||
| - | [[Category: TZZ]] | ||
[[Category: metalloenzyme]] | [[Category: metalloenzyme]] | ||
[[Category: opda]] | [[Category: opda]] | ||
[[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 Mon Mar 31 02:29:26 2008'' |
Revision as of 23:29, 30 March 2008
| |||||||
| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Aryldialkylphosphatase, with EC number 3.1.8.1 | ||||||
| Related: | 2D2G, 2D2J
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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