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

Acta Crystallogr F Struct Biol Commun. 2018 Aug 1;74(Pt 8):443-450. doi: 10.1107/S2053230X18004788. Epub 2018 Jul 26.

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

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Fucosyltransferases / chemistry*
  • Fucosyltransferases / metabolism*
  • Galactoside 2-alpha-L-fucosyltransferase
  • Humans
  • Protein Structure, Secondary
  • Protein Structure, Tertiary

Substances

  • Fucosyltransferases