5FHQ
Crystal structure of (WT) Rat Catechol-O-Methyltransferase in complex with AdoMet and 3,5-dinitrocatechol (DNC)
Summary for 5FHQ
| Entry DOI | 10.2210/pdb5fhq/pdb |
| Descriptor | Catechol O-methyltransferase, S-ADENOSYLMETHIONINE, 3,5-DINITROCATECHOL, ... (5 entities in total) |
| Functional Keywords | methyltransferase regioselectivity, transferase |
| Biological source | Rattus norvegicus (Norway Rat) |
| Cellular location | Isoform 2: Cytoplasm. Isoform 1: Cell membrane; Single-pass type II membrane protein; Extracellular side: P22734 |
| Total number of polymer chains | 1 |
| Total formula weight | 24604.38 |
| Authors | Levy, C. (deposition date: 2015-12-22, release date: 2016-02-03, Last modification date: 2024-01-10) |
| Primary citation | Law, B.J.,Bennett, M.R.,Thompson, M.L.,Levy, C.,Shepherd, S.A.,Leys, D.,Micklefield, J. Effects of Active-Site Modification and Quaternary Structure on the Regioselectivity of Catechol-O-Methyltransferase. Angew.Chem.Int.Ed.Engl., 55:2683-2687, 2016 Cited by PubMed Abstract: Catechol-O-methyltransferase (COMT), an important therapeutic target in the treatment of Parkinson's disease, is also being developed for biocatalytic processes, including vanillin production, although lack of regioselectivity has precluded its more widespread application. By using structural and mechanistic information, regiocomplementary COMT variants were engineered that deliver either meta- or para-methylated catechols. X-ray crystallography further revealed how the active-site residues and quaternary structure govern regioselectivity. Finally, analogues of AdoMet are accepted by the regiocomplementary COMT mutants and can be used to prepare alkylated catechols, including ethyl vanillin. PubMed: 26797714DOI: 10.1002/anie.201508287 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.63 Å) |
Structure validation
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