1VID
CATECHOL O-METHYLTRANSFERASE
Summary for 1VID
| Entry DOI | 10.2210/pdb1vid/pdb |
| Descriptor | CATECHOL O-METHYLTRANSFERASE, MAGNESIUM ION, S-ADENOSYLMETHIONINE, ... (5 entities in total) |
| Functional Keywords | transferase, methyltransferase, neurotransmitter degradation, transferase (methyltransferase) |
| 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 | 25395.25 |
| Authors | Vidgren, J.,Svensson, L.A.,Liljas, A. (deposition date: 1996-01-05, release date: 1996-07-11, Last modification date: 2024-02-14) |
| Primary citation | Vidgren, J.,Svensson, L.A.,Liljas, A. Crystal structure of catechol O-methyltransferase. Nature, 368:354-358, 1994 Cited by PubMed Abstract: Catechol O-methyltransferase (COMT, EC 2.1.1.6) is important in the central nervous system because it metabolizes catecholamine neurotransmitters such as dopamine. The enzyme catalyses the transfer of the methyl group from S-adenosyl-L-methionine (AdoMet) to one hydroxyl group of catechols. COMT also inactivates catechol-type compounds such as L-DOPA. With selective inhibitors of COMT in combination with L-DOPA, a new principle has been realized in the therapy of Parkinson's disease. Here we solve the atomic structure of COMT to 2.0 A resolution, which provides new insights into the mechanism of the methyl transfer reaction. The co-enzyme-binding domain is strikingly similar to that of an AdoMet-dependent DNA methylase, indicating that all AdoMet methylases may have a common structure. PubMed: 8127373DOI: 10.1038/368354a0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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