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A perspective on structural and mechanistic aspects of protein O ‐fucosylation
Author(s) -
Lira-Navarrete Erandi,
Hurtado-Guerrero Ramon
Publication year - 2018
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x18004788
Subject(s) - fucosylation , thrombospondin , egf like domain , enzyme , biochemistry , chemistry , computational biology , biology , glycoprotein , peptide sequence , gene , glycan , metalloproteinase
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.