2o7v

<table><tr><td colspan='2'>[[2o7v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acter Acter]. 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>

</td></tr><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>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2o7r|2o7r]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CXE1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=165200 ACTER])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Carboxylesterase Carboxylesterase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.1 3.1.1.1] </span></td></tr>

[[https://www.uniprot.org/uniprot/CXE1_ACTER CXE1_ACTER]] Carboxylesterase acting on esters with varying acyl chain length.<ref>PMID:17256879</ref>

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== 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&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>

[[Category: Acter]]

[[Category: Carboxylesterase]]

[[Category: Baker, E N]]

[[Category: Baker, H M]]

[[Category: Ileperuma, N R]]

[[Category: Marshall, S D]]

[[Category: Newcomb, R D]]

[[Category: Oakeshott, J G]]

[[Category: Plummer, K M]]

[[Category: Russell, R J]]

[[Category: Squire, C J]]

[[Category: Paraoxon]]