4oqd
Crystal structure of the tylM1 N,N-dimethyltransferase in complex with SAH and TDP-Qui3NMe2
Structural highlights
FunctionTYLM1_STRFR S-adenosyl-L-methionine-dependent methyltransferase involved in the biosynthesis of mycaminose, an essential structural component of the macrolide antibiotic tylosin. Involved in the last step in mycaminose biosynthesis by mediating dimethylation of the hexose C-3' amino group.[1] [2] [3] Publication Abstract from PubMedThe 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. Production of a novel N-monomethylated dideoxysugar.,Thoden JB, Holden HM Biochemistry. 2014 Feb 25;53(7):1105-7. doi: 10.1021/bi500098a. Epub 2014 Feb 11. PMID:24512254[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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