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2o7v

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[[Image:2o7v.gif|left|200px]]
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{{STRUCTURE_2o7v| PDB=2o7v | SCENE= }}
{{STRUCTURE_2o7v| PDB=2o7v | SCENE= }}
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'''Carboxylesterase AeCXE1 from Actinidia eriantha covalently inhibited by paraoxon'''
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===Carboxylesterase AeCXE1 from Actinidia eriantha covalently inhibited by paraoxon===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_17256879}}
==About this Structure==
==About this Structure==
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[[Category: Insecticide]]
[[Category: Insecticide]]
[[Category: Paraoxon]]
[[Category: Paraoxon]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:51:54 2008''

Revision as of 01:51, 29 July 2008

Image:2o7v.png

Template:STRUCTURE 2o7v

Carboxylesterase AeCXE1 from Actinidia eriantha covalently inhibited by paraoxon

Template:ABSTRACT PUBMED 17256879

About this Structure

2O7V is a Single protein structure of sequence from Actinidia eriantha. Full crystallographic information is available from OCA.

Reference

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

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