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A perspective on structural and mechanistic aspects of protein O-fucosylation
Protein O-fucosylation is an important post-translational modification (PTM) found in cysteine-rich repeats in proteins. Protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this PTM and selectively glycosylate specific residues in epidermal growth factor-like (E...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2018
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6096484/ https://www.ncbi.nlm.nih.gov/pubmed/30084393 http://dx.doi.org/10.1107/S2053230X18004788 |
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author | Lira-Navarrete, Erandi Hurtado-Guerrero, Ramon |
author_facet | Lira-Navarrete, Erandi Hurtado-Guerrero, Ramon |
author_sort | Lira-Navarrete, Erandi |
collection | PubMed |
description | Protein O-fucosylation is an important post-translational modification (PTM) found in cysteine-rich repeats in proteins. Protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this PTM and selectively glycosylate specific residues in epidermal growth factor-like (EGF) repeats and thrombospondin type I repeats (TSRs), respectively. Within the past six years, crystal structures of both enzymes have been reported, revealing important information on how they recognize protein substrates and achieve catalysis. Here, the structural information available today is summarized and how PoFUT1 and PoFUT2 employ different catalytic mechanisms is discussed. |
format | Online Article Text |
id | pubmed-6096484 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-60964842018-08-24 A perspective on structural and mechanistic aspects of protein O-fucosylation Lira-Navarrete, Erandi Hurtado-Guerrero, Ramon Acta Crystallogr F Struct Biol Commun Topical Reviews Protein O-fucosylation is an important post-translational modification (PTM) found in cysteine-rich repeats in proteins. Protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this PTM and selectively glycosylate specific residues in epidermal growth factor-like (EGF) repeats and thrombospondin type I repeats (TSRs), respectively. Within the past six years, crystal structures of both enzymes have been reported, revealing important information on how they recognize protein substrates and achieve catalysis. Here, the structural information available today is summarized and how PoFUT1 and PoFUT2 employ different catalytic mechanisms is discussed. International Union of Crystallography 2018-07-26 /pmc/articles/PMC6096484/ /pubmed/30084393 http://dx.doi.org/10.1107/S2053230X18004788 Text en © Lira-Navarrete et al. 2018 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.http://creativecommons.org/licenses/by/2.0/uk/ |
spellingShingle | Topical Reviews Lira-Navarrete, Erandi Hurtado-Guerrero, Ramon A perspective on structural and mechanistic aspects of protein O-fucosylation |
title | A perspective on structural and mechanistic aspects of protein O-fucosylation |
title_full | A perspective on structural and mechanistic aspects of protein O-fucosylation |
title_fullStr | A perspective on structural and mechanistic aspects of protein O-fucosylation |
title_full_unstemmed | A perspective on structural and mechanistic aspects of protein O-fucosylation |
title_short | A perspective on structural and mechanistic aspects of protein O-fucosylation |
title_sort | perspective on structural and mechanistic aspects of protein o-fucosylation |
topic | Topical Reviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6096484/ https://www.ncbi.nlm.nih.gov/pubmed/30084393 http://dx.doi.org/10.1107/S2053230X18004788 |
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