Structural highlights
Publication Abstract from PubMed
Structure analysis and ensemble refinement of the apo-structure of thymidine diphosphate (TDP)-rhamnose 3'-O-methyltransferase reveal a gate for substrate entry and product release. TDP-rhamnose 3'-O-methyltransferase (CalS11) catalyses a 3'-O-methylation of TDP-rhamnose, an intermediate in the biosynthesis of enediyne antitumor antibiotic calicheamicin. CalS11 operates at the sugar nucleotide stage prior to glycosylation step. Here, we present the crystal structure of the apo form of CalS11 at 1.89 A resolution. We propose that the L2 loop functions as a gate facilitating and/or providing specificity for substrate entry or promoting product release. Ensemble refinement analysis slightly improves the crystallographic refinement statistics and furthermore provides a compelling way to visualize the dynamic model of loop L2, supporting the understanding of its proposed role in catalysis.
Loop dynamics of thymidine diphosphate-rhamnose 3'-O-methyltransferase (CalS11), an enzyme in calicheamicin biosynthesis.,Han L, Singh S, Thorson JS, Phillips GN Jr Struct Dyn. 2016 Feb 18;3(1):012004. doi: 10.1063/1.4941368. eCollection 2016, Jan. PMID:26958582[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Han L, Singh S, Thorson JS, Phillips GN Jr. Loop dynamics of thymidine diphosphate-rhamnose 3'-O-methyltransferase (CalS11), an enzyme in calicheamicin biosynthesis. Struct Dyn. 2016 Feb 18;3(1):012004. doi: 10.1063/1.4941368. eCollection 2016, Jan. PMID:26958582 doi:http://dx.doi.org/10.1063/1.4941368
