6CCA
Crystal structure of DszA carbon methyltransferase
Summary for 6CCA
| Entry DOI | 10.2210/pdb6cca/pdb |
| Descriptor | DisA protein (2 entities in total) |
| Functional Keywords | methyltransferase, polyketide assembly line, disorazol, gem-dimethyl, transferase |
| Biological source | Sorangium cellulosum (Polyangium cellulosum) |
| Total number of polymer chains | 1 |
| Total formula weight | 47334.79 |
| Authors | Meinke, J.L.,Keatinge-Clay, A.T. (deposition date: 2018-02-06, release date: 2018-12-05, Last modification date: 2024-03-13) |
| Primary citation | Meinke, J.L.,Mehaffey, M.R.,Wagner, D.T.,Sun, N.,Zhang, Z.,Brodbelt, J.S.,Keatinge-Clay, A.T. Structural and Functional Studies of a gem-Dimethylating Methyltransferase from a trans-Acyltransferase Assembly Line. ACS Chem. Biol., 13:3306-3314, 2018 Cited by PubMed Abstract: The methyl substituents in products of trans-acyltransferase assembly lines are usually incorporated by S-adenosyl-methionine (SAM)-dependent methyltransferase (MT) domains. The gem-dimethyl moieties within the polyketide disorazol are installed through the iterative action of an MT in the third module of its assembly line. The 1.75-Å-resolution crystal structure of this MT helps elucidate how it catalyzes the addition of two methyl groups. Activity assays of point mutants on β-ketoacyl chains linked to an acyl carrier protein and N-acetylcysteamine provide additional insights into the roles of active site residues. The replacement of an alanine with a phenylalanine at an apparent gatekeeping position resulted in more monomethylation than dimethylation. MTs may form an interface with ketoreductases (KRs) and even mediate the docking of trans-acyltransferase assembly line polypeptides through this association. PubMed: 30371052DOI: 10.1021/acschembio.8b00733 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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