Structural characterization of O- and C-glycosylating variants of the landomycin glycosyltransferase LanGT2

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

Research output: Contribution to journalArticlepeer-review

26 Scopus citations

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.

Original languageEnglish
Pages (from-to)2811-2815
Number of pages5
JournalAngewandte Chemie - International Edition
Volume54
Issue number9
DOIs
StatePublished - Feb 23 2015

Bibliographical note

Publisher Copyright:
© 2015 Wiley-VCH Verlag GmbH & Co. KGaA.

Keywords

  • C-glycosylation
  • Carbasugars
  • Enzyme engineering
  • Friedel-Crafts alkylation
  • Glycosyltransferases

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry

Fingerprint

Dive into the research topics of 'Structural characterization of O- and C-glycosylating variants of the landomycin glycosyltransferase LanGT2'. Together they form a unique fingerprint.

Cite this