4OQE: Crystal Structure Of The Tylm1 N,n-dimethyltransferase In Complex With Sah And Tdp-fuc3nme

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.
PDB ID: 4OQEDownload
MMDB ID: 117891
PDB Deposition Date: 2014/2/8
Updated in MMDB: 2014/03
Experimental Method:
x-ray diffraction
Resolution: 2.2  Å
Source Organism:
Similar Structures:
Biological Unit for 4OQE: dimeric; determined by author and by software (PISA)
Molecular Components in 4OQE
Label Count Molecule
Proteins (2 molecules)
Dtdp-3-amino-3,6-dideoxy-alpha-d-glucopyranose N,n- Dimethyltransferase
Molecule annotation
Chemicals (4 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB