PDBsum entry 2zlb

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protein ligands links
Transferase PDB id
Protein chain
212 a.a. *
Waters ×149
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Crystal structure of apo form of rat catechol-o- methyltransferase
Structure: Catechol o-methyltransferase. Chain: a. Engineered: yes
Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562.
2.20Å     R-factor:   0.182     R-free:   0.237
Authors: E.Tsuji
Key ref: E.Tsuji et al. (2009). Crystal structures of the apo and holo form of rat catechol-O-methyltransferase. J Struct Biol, 165, 133-139. PubMed id: 19111934 DOI: 10.1016/j.jsb.2008.11.012
04-Apr-08     Release date:   07-Oct-08    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P22734  (COMT_RAT) -  Catechol O-methyltransferase
264 a.a.
212 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Catechol O-methyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol
+ catechol
= S-adenosyl-L-homocysteine
+ guaiacol
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     neurotransmitter catabolic process   2 terms 
  Biochemical function     magnesium ion binding     3 terms  


DOI no: 10.1016/j.jsb.2008.11.012 J Struct Biol 165:133-139 (2009)
PubMed id: 19111934  
Crystal structures of the apo and holo form of rat catechol-O-methyltransferase.
E.Tsuji, K.Okazaki, M.Isaji, K.Takeda.
Catechol-O-methyltransferase (COMT, EC is a monomeric enzyme that catalyzes the transfer of a methyl group from S-adenosyl-l-methionine (AdoMet) to the phenolic oxygen of substituted catechols. Although the inhibitor recognition pattern and AdoMet site have already been studied crystallographically, structural information on the catalytic cycle of COMT has not yet been obtained. In this study, comparison of the co-factor and inhibitor-bound structures revealed that the Apo form of COMT shows a conformational change and there was no cleft corresponding to the AdoMet-binding site; the overall structure was partially open form and the substrate recognition site was not clearly defined. The Holo form of COMT was similar to the quaternary structure except for the beta6-beta7 and alpha2-alpha3 ligand recognition loops. These conformational changes provide a deeper insight into the structural events occurring in reactions catalyzed by AdoMet.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19435324 K.Rutherford, and V.Daggett (2009).
A hotspot of inactivation: The A22S and V108M polymorphisms individually destabilize the active site structure of catechol O-methyltransferase.
  Biochemistry, 48, 6450-6460.  
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