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PDBsum entry 2zth

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Transferase PDB id
2zth
Jmol
Contents
Protein chain
206 a.a.
Ligands
SAM
Metals
_MG
Waters ×42

References listed in PDB file
Key reference
Title Crystal structures of the apo and holo form of rat catechol-O-Methyltransferase.
Authors E.Tsuji, K.Okazaki, M.Isaji, K.Takeda.
Ref. J Struct Biol, 2009, 165, 133-139. [DOI no: 10.1016/j.jsb.2008.11.012]
PubMed id 19111934
Abstract
Catechol-O-methyltransferase (COMT, EC 2.1.1.6) 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.
PROCHECK
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