1ez2
From Proteopedia
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| - | [[Image:1ez2.jpg|left|200px]] | + | [[Image:1ez2.jpg|left|200px]] |
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| - | '''THREE-DIMENSIONAL STRUCTURE OF THE ZINC-CONTAINING PHOSPHOTRIESTERASE WITH BOUND SUBSTRATE ANALOG DIISOPROPYLMETHYL PHOSPHONATE.''' | + | {{Structure |
| + | |PDB= 1ez2 |SIZE=350|CAPTION= <scene name='initialview01'>1ez2</scene>, resolution 1.9Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=DII:METHYLPHOSPHONIC ACID DIISOPROPYL ESTER'>DII</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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THREE-DIMENSIONAL STRUCTURE OF THE ZINC-CONTAINING PHOSPHOTRIESTERASE WITH BOUND SUBSTRATE ANALOG DIISOPROPYLMETHYL PHOSPHONATE.''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EZ2 is a [ | + | 1EZ2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Brevundimonas_diminuta Brevundimonas diminuta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EZ2 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10871616 10871616] |
[[Category: Aryldialkylphosphatase]] | [[Category: Aryldialkylphosphatase]] | ||
[[Category: Brevundimonas diminuta]] | [[Category: Brevundimonas diminuta]] | ||
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[[Category: hydrolase zinc organophosphate]] | [[Category: hydrolase zinc organophosphate]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:02:11 2008'' |
Revision as of 09:02, 20 March 2008
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| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Aryldialkylphosphatase, with EC number 3.1.8.1 | ||||||
| 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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