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PDBsum entry 2wu9

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protein ligands Protein-protein interface(s) links
Transferase PDB id
2wu9
Jmol
Contents
Protein chains
403 a.a. *
Ligands
EDO ×9
Waters ×1134
* Residue conservation analysis
PDB id:
2wu9
Name: Transferase
Title: Crystal structure of peroxisomal kat2 from arabidopsis thaliana
Structure: 3-ketoacyl-coa thiolase 2, peroxisomal. Chain: a, b. Fragment: residues 36-462. Synonym: beta-ketothiolase 2, acetyl-coa acyltransferase 2, peroxisomal 3-oxoacyl-coa thiolase 2, peroxisome defective protein 1\,3-ketoacyl-coa thiolase. Engineered: yes
Source: Arabidopsis thaliana. Thale cress. Organism_taxid: 3702. Atcc: 77500. Organelle: peroxisome. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_variant: rosettagami2(de3)
Resolution:
1.50Å     R-factor:   0.151     R-free:   0.178
Authors: V.E.Pye,C.E.Christensen,J.H.Dyer,S.Arent,A.Henriksen
Key ref: V.E.Pye et al. (2010). Peroxisomal plant 3-ketoacyl-CoA thiolase structure and activity are regulated by a sensitive redox switch. J Biol Chem, 285, 24078-24088. PubMed id: 20463027 DOI: 10.1074/jbc.M110.106013
Date:
01-Oct-09     Release date:   12-May-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q56WD9  (THIK2_ARATH) -  3-ketoacyl-CoA thiolase 2, peroxisomal
Seq:
Struc:
462 a.a.
403 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: E.C.2.3.1.16  - Acetyl-CoA C-acyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
Acyl-CoA
+ acetyl-CoA
= CoA
+ 3-oxoacyl-CoA
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   8 terms 
  Biological process     metabolic process   14 terms 
  Biochemical function     catalytic activity     5 terms  

 

 
    reference    
 
 
DOI no: 10.1074/jbc.M110.106013 J Biol Chem 285:24078-24088 (2010)
PubMed id: 20463027  
 
 
Peroxisomal plant 3-ketoacyl-CoA thiolase structure and activity are regulated by a sensitive redox switch.
V.E.Pye, C.E.Christensen, J.H.Dyer, S.Arent, A.Henriksen.
 
  ABSTRACT  
 
The breakdown of fatty acids, performed by the beta-oxidation cycle, is crucial for plant germination and sustainability. beta-oxidation involves four enzymatic reactions; the final step, where a two carbon unit is cleaved from the fatty acid, is performed by a 3-ketoacyl-CoA thiolase (KAT). The shortened fatty acid may then pass through the cycle again (until reaching acetoacetyl-CoA) or be directed to a different cellular function. Crystal structures of KAT from Arabidopsis thaliana and Helianthus annuus have been solved to 1.5 A and 1.8 A resolution respectively. The dimeric structures are very similar and exhibit a typical thiolase fold; dimer formation and active site conformation appear in an open, active, reduced state. Using an interdisciplinary approach, we confirm the potential of plant KATs to be regulated by the redox environment in the peroxisome within a physiological range. In addition, co-immunoprecipitation studies suggest an interaction between KAT and the multifunctional protein, which is responsible for the preceding two steps in beta-oxidation, that would allow a route for substrate channeling; we suggest a model for this complex based on the bacterial system.