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

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

Author information

1
Institut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21, 79104 Freiburg (Germany).

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.

KEYWORDS:

C-glycosylation; Friedel-Crafts alkylation; carbasugars; enzyme engineering; glycosyltransferases

PMID:
25581707
PMCID:
PMC4376353
DOI:
10.1002/anie.201409792
[Indexed for MEDLINE]
Free PMC Article

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