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Advances in understanding glycosyltransferases from a structural perspective

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Gloster_2014_COSB_Advances.pdf (2.422Mb)
Date
10/2014
Author
Gloster, Tracey M
Funder
The Wellcome Trust
Grant ID
095828/Z/11/Z
Keywords
QH301 Biology
SDG 3 - Good Health and Well-being
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Abstract
Glycosyltransferases (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.
Citation
Gloster , 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.2014.08.012
Publication
Current Opinion in Structural Biology
Status
Peer reviewed
DOI
https://doi.org/10.1016/j.sbi.2014.08.012
ISSN
0959-440X
Type
Journal article
Rights
© 2014 The Author. Published by Elsevier Ltd. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/3.0/).
Collections
  • University of St Andrews Research
URI
http://hdl.handle.net/10023/5535

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