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dc.contributor.authorGloster, Tracey M
dc.date.accessioned2014-10-10T11:31:03Z
dc.date.available2014-10-10T11:31:03Z
dc.date.issued2014-10
dc.identifier155018162
dc.identifier671d40fb-9541-4b68-91a0-5254d981e90f
dc.identifier25240227
dc.identifier84908673948
dc.identifier000345203000018
dc.identifier.citationGloster , T M 2014 , ' Advances in understanding glycosyltransferases from a structural perspective ' , Current Opinion in Structural Biology , vol. 28 , pp. 131-141 . https://doi.org/10.1016/j.sbi.2014.08.012en
dc.identifier.issn0959-440X
dc.identifier.urihttps://hdl.handle.net/10023/5535
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.format.extent11
dc.format.extent2540075
dc.language.isoeng
dc.relation.ispartofCurrent Opinion in Structural Biologyen
dc.subjectQH301 Biologyen
dc.subjectSDG 3 - Good Health and Well-beingen
dc.subject.lccQH301en
dc.titleAdvances in understanding glycosyltransferases from a structural perspectiveen
dc.typeJournal articleen
dc.contributor.sponsorThe Wellcome Trusten
dc.contributor.institutionUniversity of St Andrews. School of Biologyen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.identifier.doihttps://doi.org/10.1016/j.sbi.2014.08.012
dc.description.statusPeer revieweden
dc.identifier.grantnumber095828/Z/11/Zen


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