Structural highlights
Publication Abstract from PubMed
The structures of the O-glycosyltransferase LanGT2 and the engineered, CC bond-forming variant LanGT2S8Ac show how the replacement of a single loop can change the functionality of the enzyme. Crystal structures of the enzymes in complex with a nonhydrolyzable nucleotide-sugar analogue revealed that there is a conformational transition to create the binding sites for the aglycon substrate. This induced-fit transition was explored by molecular docking experiments with various aglycon substrates.
Structural Characterization of O- and C-Glycosylating Variants of the Landomycin Glycosyltransferase LanGT2.,Tam HK, Harle J, Gerhardt S, Rohr J, Wang G, Thorson JS, Bigot A, Lutterbeck M, Seiche W, Breit B, Bechthold A, Einsle O Angew Chem Int Ed Engl. 2015 Jan 7. doi: 10.1002/anie.201409792. PMID:25581707[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tam HK, Harle J, Gerhardt S, Rohr J, Wang G, Thorson JS, Bigot A, Lutterbeck M, Seiche W, Breit B, Bechthold A, Einsle O. Structural Characterization of O- and C-Glycosylating Variants of the Landomycin Glycosyltransferase LanGT2. Angew Chem Int Ed Engl. 2015 Jan 7. doi: 10.1002/anie.201409792. PMID:25581707 doi:http://dx.doi.org/10.1002/anie.201409792
