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

doi:10.1002/anie.201409792

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 journal › Article › peer-review

27 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 language	English
Pages (from-to)	2811-2815
Number of pages	5
Journal	Angewandte Chemie - International Edition
Volume	54
Issue number	9
DOIs	https://doi.org/10.1002/anie.201409792
State	Published - 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

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10.1002/anie.201409792

Cite this

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title = "Structural characterization of O- and C-glycosylating variants of the landomycin glycosyltransferase LanGT2",

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.",

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doi = "10.1002/anie.201409792",

language = "English",

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AU - Tam, Heng Keat

AU - Härle, Johannes

AU - Gerhardt, Stefan

AU - Rohr, Jürgen

AU - Wang, Guojun

AU - Thorson, Jon S.

AU - Bigot, Aurélien

AU - Lutterbeck, Monika

AU - Seiche, Wolfgang

AU - Breit, Bernhard

AU - Bechthold, Andreas

AU - Einsle, Oliver

PY - 2015/2/23

Y1 - 2015/2/23

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AB - 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.

KW - C-glycosylation

KW - Carbasugars

KW - Enzyme engineering

KW - Friedel-Crafts alkylation

KW - Glycosyltransferases

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

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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