ArticleNature chemical biology2016
A proactive role of water molecules in acceptor recognition by protein O-fucosyltransferase 2.
Article in Nature chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 62 citations in OpenAlex.
- Production of Anti-melanogenic Glucosides via Molecular Docking-guided Biotransformation of p-hydroxyphenethyl anisate.Applied biochemistry and biotechnology · 2026Article
- Crystal structure of a β1,3-Glucosyltransferase reveals an unusual substrate recognition by a two-domain GT-A fold glycosyltransferase.The Journal of biological chemistry · 2026Article
- Enzyme Reset: Water-Mediated Tautomerization Restores the Catalytic Asparagine in ProteinJournal of chemical information and modeling · 2026Article
- Structural basis of EGF-repeat O-glucosylation by the protein O-glucosyltransferase POGLUT2.The Journal of biological chemistry · 2026Article
- POFUT2 Mediated Fucosylation of JUP Enhances VEGFA Expression to Promote Angiogenesis in Colorectal Cancer.International journal of medical sciences · 2026Article
- Structure, function, and implications of fucosyltransferases in health and disease.Nature communications · 2025Review
- FUT10 and FUT11 are protein O-fucosyltransferases that modify protein EMI domains.Nature chemical biology · 2025Article
- ProteinMolecules (Basel, Switzerland) · 2025Review
- Integration of Experimental and Computational Methods to Characterize Glycoproteins.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Emerging glyco-risk prediction model to forecast response to immune checkpoint inhibitors in colorectal cancer.Journal of cancer research and clinical oncology · 2023Article
- Structure and dynamics of the Arabidopsis O-fucosyltransferase SPINDLY.Nature communications · 2023Article
- SPINDLY O-fucosylates nuclear and cytoplasmic proteins involved in diverse cellular processes in plants.Plant physiology · 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
- Structural basis for the synthesis of the core 1 structure by C1GalT1.Nature communications · 2022Article
- O-fucosylation of thrombospondin type 1 repeats is essential for ECM remodeling and signaling during bone development.Matrix biology : journal of the International Society for Matrix Biology · 2022Article
- NleB/SseK-catalyzed arginine-glycosylation and enteropathogen virulence are finely tuned by a single variable position contiguous to the catalytic machinery.Chemical science · 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
- Asparagine Tautomerization in Glycosyltransferase Catalysis. The Molecular Mechanism of ProteinACS catalysis · 2021Article
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Authors and funding
13 authors at 5 institutions in 2 countries.
Funding
Abstract
Protein O-fucosyltransferase 2 (POFUT2) is an essential enzyme that fucosylates serine and threonine residues of folded thrombospondin type 1 repeats (TSRs). To date, the mechanism by which this enzyme recognizes very dissimilar TSRs has been unclear. By engineering a fusion protein, we report the crystal structure of Caenorhabditis elegans POFUT2 (CePOFUT2) in complex with GDP and human TSR1 that suggests an inverting mechanism for fucose transfer assisted by a catalytic base and shows that nearly half of the TSR1 is embraced by CePOFUT2. A small number of direct interactions and a large network of water molecules maintain the complex. Site-directed mutagenesis demonstrates that POFUT2 fucosylates threonine preferentially over serine and relies on folded TSRs containing the minimal consensus sequence C-X-X-S/T-C. Crystallographic and mutagenesis data, together with atomic-level simulations, uncover a binding mechanism by which POFUT2 promiscuously recognizes the structural fingerprint of poorly homologous TSRs through a dynamic network of water-mediated interactions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.