2o7r
From Proteopedia
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'''Plant carboxylesterase AeCXE1 from Actinidia eriantha with acyl adduct''' | '''Plant carboxylesterase AeCXE1 from Actinidia eriantha with acyl adduct''' | ||
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[[Category: Russell, R J.]] | [[Category: Russell, R J.]] | ||
[[Category: Squire, C J.]] | [[Category: Squire, C J.]] | ||
| - | [[Category: | + | [[Category: Actinidia eriantha]] |
| - | [[Category: | + | [[Category: Alpha/beta hydrolase]] |
| - | [[Category: | + | [[Category: Carboxylesterase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:25:33 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 07:25, 4 May 2008
Plant carboxylesterase AeCXE1 from Actinidia eriantha with acyl adduct
Overview
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.
About this Structure
2O7R 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 Page seeded by OCA on Sun May 4 10:25:33 2008
