2o7v: Difference between revisions

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[[Image:2o7v.png|left|200px]]


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==Carboxylesterase AeCXE1 from Actinidia eriantha covalently inhibited by paraoxon==
The line below this paragraph, containing "STRUCTURE_2o7v", creates the "Structure Box" on the page.
<StructureSection load='2o7v' size='340' side='right'caption='[[2o7v]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2o7v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinidia_eriantha Actinidia eriantha]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O7V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O7V FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DEP:DIETHYL+PHOSPHONATE'>DEP</scene></td></tr>
{{STRUCTURE_2o7v|  PDB=2o7v  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7v OCA], [https://pdbe.org/2o7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o7v RCSB], [https://www.ebi.ac.uk/pdbsum/2o7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o7v ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CXE1_ACTER CXE1_ACTER] Carboxylesterase acting on esters with varying acyl chain length.<ref>PMID:17256879</ref>
== 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/o7/2o7v_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2o7v ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Carboxylesterases (CXEs) are widely distributed in plants, where they have been implicated in roles that include plant defense, plant development, and secondary metabolism. We have cloned, overexpressed, purified, and crystallized a carboxylesterase from the kiwifruit species Actinidia eriantha (AeCXE1). The structure of AeCXE1 was determined by X-ray crystallography at 1.4 A resolution. The crystal structure revealed that AeCXE1 is a member of the alpha/beta-hydrolase fold superfamily, most closely related structurally to the hormone-sensitive lipase subgroup. The active site of the enzyme, located in an 11 A deep hydrophobic gorge, contains the conserved catalytic triad residues Ser169, Asp276, and His306. Kinetic analysis using artificial ester substrates showed that the enzyme can hydrolyze a range of carboxylester substrates with acyl groups ranging from C2 to C16, with a preference for butyryl moieties. This preference was supported by the discovery of a three-carbon acyl adduct bound to the active site Ser169 in the native structure. AeCXE1 was also found to be inhibited by organophosphates, with paraoxon (IC50 = 1.1 muM) a more potent inhibitor than dimethylchlorophosphate (DMCP; IC50 = 9.2 muM). The structure of AeCXE1 with paraoxon bound was determined at 2.3 A resolution and revealed that the inhibitor binds covalently to the catalytic serine residue, with virtually no change in the structure of the enzyme. The structural information for AeCXE1 provides a basis for addressing the wider functional roles of carboxylesterases in plants.


===Carboxylesterase AeCXE1 from Actinidia eriantha covalently inhibited by paraoxon===
High-resolution crystal structure of plant carboxylesterase AeCXE1, from Actinidia eriantha, and its complex with a high-affinity inhibitor paraoxon.,Ileperuma NR, Marshall SD, Squire CJ, Baker HM, Oakeshott JG, Russell RJ, Plummer KM, Newcomb RD, Baker EN Biochemistry. 2007 Feb 20;46(7):1851-9. Epub 2007 Jan 26. PMID:17256879<ref>PMID:17256879</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2o7v" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_17256879}}, adds the Publication Abstract to the page
*[[Carboxylesterase 3D structures|Carboxylesterase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 17256879 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_17256879}}
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</StructureSection>
==About this Structure==
[[2o7v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Actinidia_eriantha Actinidia eriantha]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O7V OCA].
 
==Reference==
<ref group="xtra">PMID:17256879</ref><references group="xtra"/>
[[Category: Actinidia eriantha]]
[[Category: Actinidia eriantha]]
[[Category: Carboxylesterase]]
[[Category: Large Structures]]
[[Category: Baker, E N.]]
[[Category: Baker EN]]
[[Category: Baker, H M.]]
[[Category: Baker HM]]
[[Category: Ileperuma, N R.]]
[[Category: Ileperuma NR]]
[[Category: Marshall, S D.]]
[[Category: Marshall SD]]
[[Category: Newcomb, R D.]]
[[Category: Newcomb RD]]
[[Category: Oakeshott, J G.]]
[[Category: Oakeshott JG]]
[[Category: Plummer, K M.]]
[[Category: Plummer KM]]
[[Category: Russell, R J.]]
[[Category: Russell RJ]]
[[Category: Squire, C J.]]
[[Category: Squire CJ]]
Retrieved from "https://proteopedia.org/2o7v"