NMR in Glycoscience and Glycotechnology
CHAPTER 7: NMR Analysis of Glycosyltransferases
Published:15 May 2017
Special Collection: 2017 ebook collectionSeries: New Developments in NMR
T. Peters, in NMR in Glycoscience and Glycotechnology, ed. K. Kato and T. Peters, The Royal Society of Chemistry, 2017, pp. 179-193.
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Glycosyltransferases are responsible for the biosynthesis of a multitude of complex glycan chains located on cell surfaces, and representing a ″postal code system″ for cell–cell or cell–pathogen recognition. A substantial number of crystal structures of glycosyltransferases have become available showing that these enzymes undergo significant conformational changes upon binding to substrates. Yet, not much is known about the protein dynamics behind these changes. Although NMR offers powerful tools to obtain insight into dynamical processes application to glycosyltransferases has been sparse mainly because of the large size of most of these enzymes rendering especially protein NMR approaches difficult or even impossible. This review highlights studies focussing on the application of NMR experiments to study dynamical aspects of glycosyltransferases. A methodological division is made into protein-based and ligand-based techniques. From the NMR experimental data available it becomes clear that glycosyltransferases are enzymes with a large degree of plasticity.