2o7r: Difference between revisions
New page: left|200px<br /><applet load="2o7r" size="350" color="white" frame="true" align="right" spinBox="true" caption="2o7r, resolution 1.4Å" /> '''Plant carboxylesteras... |
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== | ==Plant carboxylesterase AeCXE1 from Actinidia eriantha with acyl adduct== | ||
Carboxylesterases (CXEs) are widely distributed in plants, where they have | <StructureSection load='2o7r' size='340' side='right'caption='[[2o7r]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2o7r]] 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=2O7R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O7R 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]] 1.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4PA:PROPYL+ACETATE'>4PA</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=2o7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7r OCA], [https://pdbe.org/2o7r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o7r RCSB], [https://www.ebi.ac.uk/pdbsum/2o7r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o7r 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/o7/2o7r_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=2o7r 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. | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2o7r" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Carboxylesterase 3D structures|Carboxylesterase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Actinidia eriantha]] | [[Category: Actinidia eriantha]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Baker EN]] | |||
[[Category: Baker | [[Category: Baker HM]] | ||
[[Category: Baker | [[Category: Ileperuma NR]] | ||
[[Category: Ileperuma | [[Category: Marshall SD]] | ||
[[Category: Marshall | [[Category: Newcomb RD]] | ||
[[Category: Newcomb | [[Category: Oakeshott JG]] | ||
[[Category: Oakeshott | [[Category: Plummer KM]] | ||
[[Category: Plummer | [[Category: Russell RJ]] | ||
[[Category: Russell | [[Category: Squire CJ]] | ||
[[Category: Squire | |||
