Open access
Date
2023-04Type
- Review Article
Abstract
Glycosyltransferases of the C superfamily (GT-Cs) are enzymes found in all domains of life. They catalyse the stepwise synthesis of oligosaccharides or the transfer of assembled glycans from lipid-linked donor substrates to acceptor proteins. The processes mediated by GT-Cs are required for C-, N- and O-linked glycosylation, all of which are essential post-translational modifications in higher-order eukaryotes. Until recently, GT-Cs were thought to share a conserved structural module of 7 transmembrane helices; however, recently determined GT-C structures revealed novel folds. Here we analyse the growing diversity of GT-C folds and discuss the emergence of two subclasses, termed GT-CA and GT-CB. Further substrate-bound structures are needed to facilitate a molecular understanding of glycan recognition and catalysis in these two subclasses. Show more
Permanent link
https://doi.org/10.3929/ethz-b-000601193Publication status
publishedExternal links
Journal / series
Current Opinion in Structural BiologyVolume
Pages / Article No.
Publisher
ElsevierOrganisational unit
03652 - Locher, Kaspar / Locher, Kaspar
Funding
196862 - Structural and mechanistic investigations of membrane-integral enzymes involved in eukaryotic protein N-glycosylation pathway (SNF)
More
Show all metadata