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dc.contributor.authorGloster, Tracey M
dc.identifier.citationGloster , T M 2014 , ' Advances in understanding glycosyltransferases from a structural perspective ' , Current Opinion in Structural Biology , vol. 28 , pp. 131-141 .
dc.identifier.otherPURE: 155018162
dc.identifier.otherPURE UUID: 671d40fb-9541-4b68-91a0-5254d981e90f
dc.identifier.otherPubMed: 25240227
dc.identifier.otherScopus: 84908673948
dc.identifier.otherWOS: 000345203000018
dc.description.abstractGlycosyltransferases (GTs), the enzymes that catalyse glycosidic bond formation, create a diverse range of saccharides and glycoconjugates in nature. Understanding GTs at the molecular level, through structural and kinetic studies, is important for gaining insights into their function. In addition, this understanding can help identify those enzymes which are involved in diseases, or that could be engineered to synthesize biologically or medically relevant molecules. This review describes how structural data, obtained in the last 3-4 years, have contributed to our understanding of the mechanisms of action and specificity of GTs. Particular highlights include the structure of a bacterial oligosaccharyltransferase, which provides insights into N-linked glycosylation, the structure of the human O-GlcNAc transferase, and the structure of a bacterial integral membrane protein complex that catalyses the synthesis of cellulose, the most abundant organic molecule in the biosphere.
dc.relation.ispartofCurrent Opinion in Structural Biologyen
dc.rights© 2014 The Author. Published by Elsevier Ltd. This is an open access article under the CC BY license (
dc.subjectQH301 Biologyen
dc.subjectSDG 3 - Good Health and Well-beingen
dc.titleAdvances in understanding glycosyltransferases from a structural perspectiveen
dc.typeJournal articleen
dc.contributor.sponsorThe Wellcome Trusten
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews. School of Biologyen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.description.statusPeer revieweden

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