Structural Characterization of O- and C-Glycosylating Variants of the Landomycin Glycosyltransferase LanGT2
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...
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Veröffentlicht in: | Angewandte Chemie International Edition 2015-02, Vol.54 (9), p.2811-2815 |
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Sprache: | eng |
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Zusammenfassung: | 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.
Oh to see glycosyl transfer: Crystal 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. |
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ISSN: | 1433-7851 1521-3773 |
DOI: | 10.1002/anie.201409792 |