1ez2
From Proteopedia
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|PDB= 1ez2 |SIZE=350|CAPTION= <scene name='initialview01'>1ez2</scene>, resolution 1.9Å | |PDB= 1ez2 |SIZE=350|CAPTION= <scene name='initialview01'>1ez2</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=DII:METHYLPHOSPHONIC+ACID+DIISOPROPYL+ESTER'>DII</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=[[1eyw|1EYW]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ez2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ez2 OCA], [http://www.ebi.ac.uk/pdbsum/1ez2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ez2 RCSB]</span> | ||
}} | }} | ||
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[[Category: Hong, S B.]] | [[Category: Hong, S B.]] | ||
[[Category: Raushel, F M.]] | [[Category: Raushel, F M.]] | ||
| - | [[Category: DII]] | ||
| - | [[Category: ZN]] | ||
[[Category: hydrolase zinc organophosphate]] | [[Category: hydrolase zinc organophosphate]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:12:34 2008'' |
Revision as of 17:12, 30 March 2008
| |||||||
| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Aryldialkylphosphatase, with EC number 3.1.8.1 | ||||||
| Related: | 1EYW
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THREE-DIMENSIONAL STRUCTURE OF THE ZINC-CONTAINING PHOSPHOTRIESTERASE WITH BOUND SUBSTRATE ANALOG DIISOPROPYLMETHYL PHOSPHONATE.
Overview
Phosphotriesterase (PTE) from Pseudomonas diminuta catalyzes the detoxification of organophosphates such as the widely utilized insecticide paraoxon and the chemical warfare agent sarin. The three-dimensional structure of the enzyme is known from high resolution x-ray crystallographic analyses. Each subunit of the homodimer folds into a so-called TIM barrel, with eight strands of parallel beta-sheet. The two zinc ions required for activity are positioned at the C-terminal portion of the beta-barrel. Here, we describe the three-dimensional structure of PTE complexed with the inhibitor diisopropyl methyl phosphonate, which serves as a mimic for sarin. Additionally, the structure of the enzyme complexed with triethyl phosphate is also presented. In the case of the PTE-diisopropyl methyl phosphonate complex, the phosphoryl oxygen of the inhibitor coordinates to the more solvent-exposed zinc ion (2.5 A), thereby lending support to the presumed catalytic mechanism involving metal coordination of the substrate. In the PTE-triethyl phosphate complex, the phosphoryl oxygen of the inhibitor is positioned at 3.4 A from the more solvent-exposed zinc ion. The two structures described in this report provide additional molecular understanding for the ability of this remarkable enzyme to hydrolyze such a wide range of organophosphorus substrates.
About this Structure
1EZ2 is a Single protein structure of sequence from Brevundimonas diminuta. Full crystallographic information is available from OCA.
Reference
The binding of substrate analogs to phosphotriesterase., Benning MM, Hong SB, Raushel FM, Holden HM, J Biol Chem. 2000 Sep 29;275(39):30556-60. PMID:10871616
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