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Structural Characterization of O‐ and C‐Glycosylating Variants of the Landomycin Glycosyltransferase LanGT2
Author(s) -
Tam Heng Keat,
Härle Johannes,
Gerhardt Stefan,
Rohr Jürgen,
Wang Guojun,
Thorson Jon S.,
Bigot Aurélien,
Lutterbeck Monika,
Seiche Wolfgang,
Breit Bernhard,
Bechthold Andreas,
Einsle Oliver
Publication year - 2015
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201409792
Subject(s) - glycosyltransferase , stereochemistry , chemistry , enzyme , transition (genetics) , docking (animal) , nucleotide , nucleotide sugar , substrate (aquarium) , substrate specificity , biochemistry , biology , gene , medicine , ecology , nursing
Abstract The structures of the O‐glycosyltransferase LanGT2 and the engineered, CC 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.