Download MendeleyStructural Characterization of O- and C-Glycosylating Variants of the Landomycin Glycosyltransferase LanGT2.
Tam, H.K., Harle, J., Gerhardt, S., Rohr, J., Wang, G., Thorson, J.S., Bigot, A., Lutterbeck, M., Seiche, W., Breit, B., Bechthold, A., Einsle, O.(2015) Angew Chem Int Ed Engl 54: 2811-2815
- PubMed: 25581707
- DOI: https://doi.org/10.1002/anie.201409792
- Primary Citation of Related Structures:
4RIE, 4RIF, 4RIG, 4RIH, 4RII - PubMed Abstract:
The structures of the O-glycosyltransferase LanGT2 and the engineered, C-C 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.
Organizational Affiliation:
Institut f¨¹r Biochemie, Albert-Ludwigs-Universit?t Freiburg, Albertstrasse 21, 79104 Freiburg (Germany).
