We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2o7r

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2o7r.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2o7r.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2o7r| PDB=2o7r | SCENE= }}
{{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==
==About this Structure==
Line 35: Line 39:
[[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

Image:2o7r.png

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2o7r"
Personal tools