2o7r: Difference between revisions

Revision as of 15:32, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2o7r.png

Template:STRUCTURE 2o7r

Plant carboxylesterase AeCXE1 from Actinidia eriantha with acyl adductPlant carboxylesterase AeCXE1 from Actinidia eriantha with acyl adduct

Template:ABSTRACT PUBMED 17256879

About this StructureAbout this Structure

2O7R is a Single protein structure of sequence from Actinidia eriantha. Full crystallographic information is available from OCA.

ReferenceReference

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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2o7r.gif|left|200px]]
+{{Seed}}
+[[Image:2o7r.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2o7r|  PDB=2o7r  |  SCENE=  }}
-'''Plant carboxylesterase AeCXE1 from Actinidia eriantha with acyl adduct'''
+===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.
+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.
+-->
+{{ABSTRACT_PUBMED_17256879}}
 ==About this Structure==
@@ Line 35: / Line 39: @@
 [[Category: Alpha/beta hydrolase]]
 [[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''