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

Angew Chem Int Ed Engl. 2015 Feb 23;54(9):2811-5. doi: 10.1002/anie.201409792. Epub 2015 Jan 7.


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.

Keywords: C-glycosylation; Friedel-Crafts alkylation; carbasugars; enzyme engineering; glycosyltransferases.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallography, X-Ray
  • Glycosylation
  • Glycosyltransferases / chemistry
  • Glycosyltransferases / metabolism*
  • Molecular Docking Simulation
  • Protein Conformation
  • Protein Engineering


  • Glycosyltransferases