This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1eyw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1eyw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eyw, resolution 1.90&Aring;" /> '''THREE-DIMENSIONAL ST...)
Current revision (10:08, 20 March 2024) (edit) (undo)
 
(17 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1eyw.gif|left|200px]]<br /><applet load="1eyw" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1eyw, resolution 1.90&Aring;" />
 
-
'''THREE-DIMENSIONAL STRUCTURE OF THE ZINC-CONTAINING PHOSPHOTRIESTERASE WITH BOUND SUBSTRATE ANALOG TRIETHYLPHOSPHATE'''<br />
 
-
==Overview==
+
==THREE-DIMENSIONAL STRUCTURE OF THE ZINC-CONTAINING PHOSPHOTRIESTERASE WITH BOUND SUBSTRATE ANALOG TRIETHYLPHOSPHATE==
-
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.
+
<StructureSection load='1eyw' size='340' side='right'caption='[[1eyw]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1eyw]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EYW FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=PEL:2-PHENYL-ETHANOL'>PEL</scene>, <scene name='pdbligand=TEN:TRIETHYL+PHOSPHATE'>TEN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eyw OCA], [https://pdbe.org/1eyw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eyw RCSB], [https://www.ebi.ac.uk/pdbsum/1eyw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eyw ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/OPD_BREDI OPD_BREDI] Has an unusual substrate specificity for synthetic organophosphate triesters and phosphorofluoridates. All of the phosphate triesters found to be substrates are synthetic compounds. The identity of any naturally occurring substrate for the enzyme is unknown. Has no detectable activity with phosphate monoesters or diesters and no activity as an esterase or protease. It catalyzes the hydrolysis of the insecticide paraoxon at a rate approaching the diffusion limit and thus appears to be optimally evolved for utilizing this synthetic substrate.
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ey/1eyw_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1eyw ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
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 ZN, TEN and PEL 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EYW OCA].
+
*[[Phosphotriesterase 3D structures|Phosphotriesterase 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
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]
+
-
[[Category: Aryldialkylphosphatase]]
+
[[Category: Brevundimonas diminuta]]
[[Category: Brevundimonas diminuta]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Benning, M.M.]]
+
[[Category: Benning MM]]
-
[[Category: Holden, H.M.]]
+
[[Category: Holden HM]]
-
[[Category: Hong, S.B.]]
+
[[Category: Hong S-B]]
-
[[Category: Raushel, F.M.]]
+
[[Category: Raushel FM]]
-
[[Category: PEL]]
+
-
[[Category: TEN]]
+
-
[[Category: ZN]]
+
-
[[Category: hydrolase]]
+
-
[[Category: organophosphate]]
+
-
[[Category: zinc]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:26:49 2007''
+

Current revision

THREE-DIMENSIONAL STRUCTURE OF THE ZINC-CONTAINING PHOSPHOTRIESTERASE WITH BOUND SUBSTRATE ANALOG TRIETHYLPHOSPHATE

PDB ID 1eyw

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1eyw"
Personal tools