Structural Characterization of O- and C-Glycosylating Variants of the Landomycin Glycosyltransferase LanGT2

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...

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Veröffentlicht in:Angewandte Chemie International Edition 2015-02, Vol.54 (9), p.2811-2815
Hauptverfasser: 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
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Sprache:eng
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Zusammenfassung: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. Oh to see glycosyl transfer: Crystal 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.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201409792