ArticleThe EMBO journal2012
Structure of human POFUT2: insights into thrombospondin type 1 repeat fold and O-fucosylation.
Article in The EMBO journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 71 citations in OpenAlex.
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- Exploiting human fucosyltransferase 8 allostery with a covalent inhibitor for core fucosylation suppression.Nature communications · 2026Article
- Molecular basis of collagen galactosylation by GLT25D1.Nature communications · 2026Article
- Structure, function, and implications of fucosyltransferases in health and disease.Nature communications · 2025Review
- Fucosylation in digestive inflammatory diseases and cancers: From mechanical studies to clinical translation.Genes & diseases · 2025Review
- Comparative evaluation of methods for the prediction of protein-ligand binding sites.Journal of cheminformatics · 2024Article
- Review
- The Multifaceted Role of FUT8 in Tumorigenesis: From Pathways to Potential Clinical Applications.International journal of molecular sciences · 2024Review
- Fucose as a nutrient ligand for Dikarya and a building block of early diverging lineages.IMA fungus · 2023Article
- Preliminary study on the mechanism of POFUT1 in colorectal cancer.Medical oncology (Northwood, London, England) · 2023Article
- Structure and dynamics of the Arabidopsis O-fucosyltransferase SPINDLY.Nature communications · 2023Article
- Hepatic transcript profiling in beef cattle: Effects of rumen-protected niacin supplementation.PloS one · 2023Article
- Structural insights into mechanism and specificity of the plant protein O-fucosyltransferase SPINDLY.Nature communications · 2022Article
- The Essential Role of Water Molecules in the Reaction Mechanism of Protein O-Fucosyltransferase 2.Angewandte Chemie (International ed. in English) · 2022Article
- O-fucosylation stabilizes the TSR3 motif in thrombospondin-1 by interacting with nearby amino acids and protecting a disulfide bond.The Journal of biological chemistry · 2022Article
- Article
- NleB/SseK-catalyzed arginine-glycosylation and enteropathogen virulence are finely tuned by a single variable position contiguous to the catalytic machinery.Chemical science · 2021Article
- A spoonful of L-fucose-an efficient therapy for GFUS-CDG, a new glycosylation disorder.EMBO molecular medicine · 2021Article
- Structural Insights in Mammalian Sialyltransferases and Fucosyltransferases: We Have Come a Long Way, but It Is Still a Long Way Down.Molecules (Basel, Switzerland) · 2021Review
- A Glycolipid Glycosyltransferase with Broad Substrate Specificity from the Marine Bacterium "Applied and environmental microbiology · 2021Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein O-fucosylation is a post-translational modification found on serine/threonine residues of thrombospondin type 1 repeats (TSR). The fucose transfer is catalysed by the protein O-fucosyltransferase 2 (POFUT2) and >40 human proteins contain the TSR consensus sequence for POFUT2-dependent fucosylation. To better understand O-fucosylation on TSR, we carried out a structural and functional analysis of human POFUT2 and its TSR substrate. Crystal structures of POFUT2 reveal a variation of the classical GT-B fold and identify sugar donor and TSR acceptor binding sites. Structural findings are correlated with steady-state kinetic measurements of wild-type and mutant POFUT2 and TSR and give insight into the catalytic mechanism and substrate specificity. By using an artificial mini-TSR substrate, we show that specificity is not primarily encoded in the TSR protein sequence but rather in the unusual 3D structure of a small part of the TSR. Our findings uncover that recognition of distinct conserved 3D fold motifs can be used as a mechanism to achieve substrate specificity by enzymes modifying completely folded proteins of very wide sequence diversity and biological function.
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