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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...

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Autores principales: Lira-Navarrete, Erandi, Hurtado-Guerrero, Ramon
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2018
Materias:
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.
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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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