Summary for 3O7W
| Entry DOI | 10.2210/pdb3o7w/pdb |
| Descriptor | Leucine carboxyl methyltransferase 1, GLYCEROL, S-ADENOSYLMETHIONINE, ... (5 entities in total) |
| Functional Keywords | modified rossmann fold, transferase, pp2a |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 34424.46 |
| Authors | Tsai, M.L.,Cronin, N.,Djordjevic, S. (deposition date: 2010-08-01, release date: 2010-09-08, Last modification date: 2024-03-20) |
| Primary citation | Tsai, M.L.,Cronin, N.,Djordjevic, S. The structure of human leucine carboxyl methyltransferase 1 that regulates protein phosphatase PP2A Acta Crystallogr.,Sect.D, 67:14-24, 2011 Cited by PubMed Abstract: Leucine carboxyl methyltransferase 1 (LCMT1) methylates the terminal carboxyl group of the leucine 309 residue of human protein phosphatase 2A (PP2A). PP2A, a key regulator of many cellular processes, has recently generated additional interest as a potential cancer-therapeutic target. The status of PP2A methylation impacts upon the selection of the regulatory subunit by the PP2A core enzyme, thus directing its activity and subcellular localization. An X-ray crystal structure of human LCMT1 protein in complex with the cofactor S-adenosylmethionine (AdoMet) has been solved to a resolution of 2 Å. The structure enables the postulation of a mode of interaction with protein phosphatase PP2A and provides a platform for further functional studies of the regulation of methylation of PP2A. PubMed: 21206058DOI: 10.1107/S0907444910042204 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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