Work

Structural Characterization of O‐ and C‐Glycosylating Variants of the Landomycin Glycosyltransferase LanGT2

Year: 2015

Type: article

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.

Source: Angewandte Chemie International Edition

DOI: 10.1002/anie.201409792

Authors: Heng Keat Tam, Johannes Härle, Stefan Gerhardt, Jürgen Rohr, Guojun Wang, Jon S. Thorson, Aurélien Bigot, Monika Lutterbeck, Wolfgang Seiche, Bernhard Breit, Andreas Bechthold, Oliver Einsle

Institutions: University of Freiburg, University of Kentucky

Language: English

Topic: Carbohydrate Chemistry and Synthesis

Subfield: Organic Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: green

Funders: National Institutes of Health, National Cancer Institute, National Institute of General Medical Sciences, National Institute of Allergy and Infectious Diseases, National Center for Advancing Translational Sciences

Awards: G1221807143, BIOSYNTHETIC KEY STEPS OF ANGUCYCLINE ANTITUMOR DRUGS, Novel aureolic acid type antitumor agents, G5658248490, Kentucky Center for Clinical and Translational Science, In Vitro Glycorandomization of Natural Products, Kentucky Center for Clinical and Translational Science, Exploring Post-Type II PKS Frame Modifications

OpenAlex ID: W2103794549

FWCI: 1.827

Cites: 42

Cited by: 31

Related to: 10