4OQD
Crystal structure of the tylM1 N,N-dimethyltransferase in complex with SAH and TDP-Qui3NMe2
Summary for 4OQD
| Entry DOI | 10.2210/pdb4oqd/pdb |
| Related | 4OQE |
| Descriptor | dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferase, S-ADENOSYL-L-HOMOCYSTEINE, TDP-3,6-dideoxy-3-N,N-dimethylglucose, ... (4 entities in total) |
| Functional Keywords | sam methyltransferase, n-methyltransferase, s-adenosylmethionine, transferase |
| Biological source | Streptomyces fradiae |
| Total number of polymer chains | 4 |
| Total formula weight | 117990.78 |
| Authors | Thoden, J.B.,Holden, H.M. (deposition date: 2014-02-08, release date: 2014-02-26, Last modification date: 2023-09-20) |
| Primary citation | Thoden, J.B.,Holden, H.M. Production of a novel N-monomethylated dideoxysugar. Biochemistry, 53:1105-1107, 2014 Cited by PubMed Abstract: The importance of unusual deoxysugars in biology has become increasingly apparent over the past decade. Some, for example, play key roles in the physiological activities of the natural products to which they are attached. Here we describe a study of TylM1, a dimethyltransferase from Streptomyces fradiae involved in the production of dTDP-mycaminose. From this investigation, the manner in which the enzyme binds its dimethylated product has been revealed. More significantly, by providing the enzyme with an alternative substrate, it was possible to produce a monomethylated product not observed in nature. This has important ramifications for the production of unique carbohydrates that may prove useful in drug design. PubMed: 24512254DOI: 10.1021/bi500098a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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