A perspective on structural and mechanistic aspects of protein O-fucosylation

Erandi Lira-Navarrete; Ramon Hurtado-Guerrero

doi:10.1107/S2053230X18004788

A perspective on structural and mechanistic aspects of protein O-fucosylation

Erandi Lira-Navarrete, Ramon Hurtado-Guerrero^*

^*Corresponding author for this work

Glycomics Program

7 Citations (Scopus)

32 Downloads (Pure)

Abstract

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.

Original language	English
Journal	Acta Crystallographica Section F: Structural Biology Communications
Volume	74
Issue number	8
Pages (from-to)	443-450
Number of pages	8
ISSN	2053-230X
DOIs	https://doi.org/10.1107/S2053230X18004788
Publication status	Published - 2018

Keywords

EGF repeats
enzyme mechanisms
epidermal growth factor-like repeats
GDP-fucose
O-fucosylation
protein O-fucosyltransferases
thrombospondin type I repeats
TSRs

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A perspective on structural and mechanistic aspects of protein O-fucosylationFinal published version, 1.92 MBLicence: CC BY

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title = "A perspective on structural and mechanistic aspects of protein O-fucosylation",

abstract = "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.",

keywords = "EGF repeats, enzyme mechanisms, epidermal growth factor-like repeats, GDP-fucose, O-fucosylation, protein O-fucosyltransferases, thrombospondin type I repeats, TSRs",

author = "Erandi Lira-Navarrete and Ramon Hurtado-Guerrero",

year = "2018",

doi = "10.1107/S2053230X18004788",

language = "English",

volume = "74",

pages = "443--450",

journal = "Acta Crystallographica Section F: Structural Biology Communications",

issn = "2053-230X",

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TY - JOUR

T1 - A perspective on structural and mechanistic aspects of protein O-fucosylation

AU - Lira-Navarrete, Erandi

AU - Hurtado-Guerrero, Ramon

PY - 2018

Y1 - 2018

N2 - 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.

AB - 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.

KW - EGF repeats

KW - enzyme mechanisms

KW - epidermal growth factor-like repeats

KW - GDP-fucose

KW - O-fucosylation

KW - protein O-fucosyltransferases

KW - thrombospondin type I repeats

KW - TSRs

U2 - 10.1107/S2053230X18004788

DO - 10.1107/S2053230X18004788

M3 - Review

C2 - 30084393

AN - SCOPUS:85051271215

SN - 2053-230X

VL - 74

SP - 443

EP - 450

JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

IS - 8

ER -

A perspective on structural and mechanistic aspects of protein O-fucosylation

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Keywords

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