1eyw

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[[Image:1eyw.gif|left|200px]]<br /><applet load="1eyw" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1eyw.gif|left|200px]]
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caption="1eyw, resolution 1.90&Aring;" />
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'''THREE-DIMENSIONAL STRUCTURE OF THE ZINC-CONTAINING PHOSPHOTRIESTERASE WITH BOUND SUBSTRATE ANALOG TRIETHYLPHOSPHATE'''<br />
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{{Structure
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|PDB= 1eyw |SIZE=350|CAPTION= <scene name='initialview01'>1eyw</scene>, resolution 1.90&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=TEN:TRIETHYL+PHOSPHATE'>TEN</scene> and <scene name='pdbligand=PEL:2-PHENYL-ETHANOL'>PEL</scene>
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|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]
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|GENE=
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}}
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'''THREE-DIMENSIONAL STRUCTURE OF THE ZINC-CONTAINING PHOSPHOTRIESTERASE WITH BOUND SUBSTRATE ANALOG TRIETHYLPHOSPHATE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1EYW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Brevundimonas_diminuta Brevundimonas diminuta] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=TEN:'>TEN</scene> and <scene name='pdbligand=PEL:'>PEL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EYW OCA].
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1EYW 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=1EYW OCA].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10871616 10871616]
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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: zinc]]
[[Category: zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:33:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:02:07 2008''

Revision as of 09:02, 20 March 2008

Image:1eyw.gif


PDB ID 1eyw

Drag the structure with the mouse to rotate
, resolution 1.90Å
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 TRIETHYLPHOSPHATE


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

1EYW 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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