PDBsum entry 2o7r

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protein ligands links
Hydrolase PDB id
Protein chain
307 a.a. *
Waters ×217
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Plant carboxylesterase aecxe1 from actinidia eriantha with acyl adduct
Structure: Cxe carboxylesterase. Chain: a. Engineered: yes
Source: Actinidia eriantha. Organism_taxid: 165200. Gene: cxe1. Expressed in: escherichia coli. Expression_system_taxid: 562.
1.40Å     R-factor:   0.200     R-free:   0.218
Authors: N.R.Ileperuma,S.D.Marshall,C.J.Squire,H.M.Baker, J.G.Oakeshott,R.J.Russell,K.M.Plummer,R.D.Newcomb,E.N.Baker
Key ref:
N.R.Ileperuma et al. (2007). High-resolution crystal structure of plant carboxylesterase AeCXE1, from Actinidia eriantha, and its complex with a high-affinity inhibitor paraoxon. Biochemistry, 46, 1851-1859. PubMed id: 17256879 DOI: 10.1021/bi062046w
11-Dec-06     Release date:   27-Feb-07    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q0ZPV7  (CXE1_ACTER) -  Carboxylesterase 1
335 a.a.
307 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Carboxylesterase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: A carboxylic ester + H2O = an alcohol + a carboxylate
carboxylic ester
+ H(2)O
= alcohol
+ carboxylate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   1 term 
  Biochemical function     carboxylic ester hydrolase activity     2 terms  


DOI no: 10.1021/bi062046w Biochemistry 46:1851-1859 (2007)
PubMed id: 17256879  
High-resolution crystal structure of plant carboxylesterase AeCXE1, from Actinidia eriantha, and its complex with a high-affinity inhibitor paraoxon.
N.R.Ileperuma, S.D.Marshall, C.J.Squire, H.M.Baker, J.G.Oakeshott, R.J.Russell, K.M.Plummer, R.D.Newcomb, E.N.Baker.
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.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21315388 E.J.Souleyre, S.D.Marshall, J.G.Oakeshott, R.J.Russell, K.M.Plummer, and R.D.Newcomb (2011).
Biochemical characterisation of MdCXE1, a carboxylesterase from apple that is expressed during fruit ripening.
  Phytochemistry, 72, 564-571.  
20237672 J.D.Sellars, M.Landrum, A.Congreve, D.P.Dixon, J.A.Mosely, A.Beeby, R.Edwards, and P.G.Steel (2010).
Fluorescence quenched quinone methide based activity probes--a cautionary tale.
  Org Biomol Chem, 8, 1610-1618.  
19037316 A.Shimada, M.Ueguchi-Tanaka, T.Nakatsu, M.Nakajima, Y.Naoe, H.Ohmiya, H.Kato, and M.Matsuoka (2008).
Structural basis for gibberellin recognition by its receptor GID1.
  Nature, 456, 520-523.
PDB codes: 3ebl 3ed1
19037309 K.Murase, Y.Hirano, T.P.Sun, and T.Hakoshima (2008).
Gibberellin-induced DELLA recognition by the gibberellin receptor GID1.
  Nature, 456, 459-463.
PDB codes: 2zsh 2zsi
18655731 R.N.Crowhurst, A.P.Gleave, E.A.MacRae, C.Ampomah-Dwamena, R.G.Atkinson, L.L.Beuning, S.M.Bulley, D.Chagne, K.B.Marsh, A.J.Matich, M.Montefiori, R.D.Newcomb, R.J.Schaffer, B.Usadel, A.C.Allan, H.L.Boldingh, J.H.Bowen, M.W.Davy, R.Eckloff, A.R.Ferguson, L.G.Fraser, E.Gera, R.P.Hellens, B.J.Janssen, K.Klages, K.R.Lo, R.M.MacDiarmid, B.Nain, M.A.McNeilage, M.Rassam, A.C.Richardson, E.H.Rikkerink, G.S.Ross, R.Schröder, K.C.Snowden, E.J.Souleyre, M.D.Templeton, E.F.Walton, D.Wang, M.Y.Wang, Y.Y.Wang, M.Wood, R.Wu, Y.K.Yauk, and W.A.Laing (2008).
Analysis of expressed sequence tags from Actinidia: applications of a cross species EST database for gene discovery in the areas of flavor, health, color and ripening.
  BMC Genomics, 9, 351.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.