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| - | [[Image:2o7r.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2o7r.png|left|200px]] |
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| | {{STRUCTURE_2o7r| PDB=2o7r | SCENE= }} | | {{STRUCTURE_2o7r| PDB=2o7r | SCENE= }} |
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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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| - | ==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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17256879}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17256879 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17256879}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Alpha/beta hydrolase]] | | [[Category: Alpha/beta hydrolase]] |
| | [[Category: Carboxylesterase]] | | [[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 Sun Jul 27 15:32:51 2008'' |
Revision as of 12:32, 27 July 2008
Template:STRUCTURE 2o7r
Plant carboxylesterase AeCXE1 from Actinidia eriantha with acyl adduct
Template:ABSTRACT PUBMED 17256879
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 Jul 27 15:32:51 2008
