ArticleThe Journal of biological chemistry2013
Enzymatic basis for N-glycan sialylation: structure of rat α2,6-sialyltransferase (ST6GAL1) reveals conserved and unique features for glycan sialylation.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
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Who cites it
91 citing papers in PubMed, 131 citations in OpenAlex.
- Sulfonylurea Bioisosteres of Sulfonic Acid in JFD 00458-Based ST6GAL1 Inhibitors Enhance Membrane Permeability.ChemMedChem · 2026Article
- Modeling glycans with AlphaFold 3: capabilities, caveats, and limitations.Glycobiology · 2025Article
- Mammalian Cell Surface Display for High-Throughput Protein Engineering of Glycosyltransferases.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- The Role of Glycans in Human Immunity-A Sweet Code.Molecules (Basel, Switzerland) · 2025Review
- Temporal dynamics of IgG-mediated immunometabolic dysfunction: from acute obesity to chronic aging.Frontiers in immunology · 2025Review
- Unique Glycans in Synaptic Glycoproteins in Mouse Brain.ACS chemical neuroscience · 2024Article
- Protein N -Glycans in Healthy and Sclerotic Glomeruli in Diabetic Kidney Disease.Journal of the American Society of Nephrology : JASN · 2024Article
- Chemoenzymatic Synthesis of SulfatedJACS Au · 2024Article
- Putative rhamnogalacturonan-II glycosyltransferase identified through callus gene editing which bypasses embryo lethality.Plant physiology · 2024Article
- Probing altered receptor specificities of antigenically drifting human H3N2 viruses by chemoenzymatic synthesis, NMR, and modeling.Nature communications · 2024Article
- Article
- Review
- Glycosyltransferase 8 domain-containing protein 1 (GLT8D1) is a UDP-dependent galactosyltransferase.Scientific reports · 2023Article
- Neural-specific alterations in glycosphingolipid biosynthesis and cell signaling associated with two human ganglioside GM3 synthase deficiency variants.Human molecular genetics · 2023Article
- Article
- Structural basis for Lewis antigen synthesis by the α1,3-fucosyltransferase FUT9.Nature chemical biology · 2023Article
- The vertebrate sialylation machinery: structure-function and molecular evolution of GT-29 sialyltransferases.Glycoconjugate journal · 2023Review
- The disulfide catalyst QSOX1 maintains the colon mucosal barrier by regulating Golgi glycosyltransferases.The EMBO journal · 2023Article
- α2,6 Sialylation mediated by ST6GAL1 promotes glioblastoma growth.JCI insight · 2022Article
- Site-selective sulfation of N-glycans by human GlcNAc-6-O-sulfotransferase 1 (CHST2) and chemoenzymatic synthesis of sulfated antibody glycoforms.Bioorganic chemistry · 2022Article
31 more citing papers are in PubMed but not listed here.
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Authors and funding
19 authors at 3 institutions in 4 countries.
Funding
Abstract
Glycan structures on glycoproteins and glycolipids play critical roles in biological recognition, targeting, and modulation of functions in animal systems. Many classes of glycan structures are capped with terminal sialic acid residues, which contribute to biological functions by either forming or masking glycan recognition sites on the cell surface or secreted glycoconjugates. Sialylated glycans are synthesized in mammals by a single conserved family of sialyltransferases that have diverse linkage and acceptor specificities. We examined the enzymatic basis for glycan sialylation in animal systems by determining the crystal structures of rat ST6GAL1, an enzyme that creates terminal α2,6-sialic acid linkages on complex-type N-glycans, at 2.4 Å resolution. Crystals were obtained from enzyme preparations generated in mammalian cells. The resulting structure revealed an overall protein fold broadly resembling the previously determined structure of pig ST3GAL1, including a CMP-sialic acid-binding site assembled from conserved sialylmotif sequence elements. Significant differences in structure and disulfide bonding patterns were found outside the sialylmotif sequences, including differences in residues predicted to interact with the glycan acceptor. Computational substrate docking and molecular dynamics simulations were performed to predict and evaluate the CMP-sialic acid donor and glycan acceptor interactions, and the results were compared with kinetic analysis of active site mutants. Comparisons of the structure with pig ST3GAL1 and a bacterial sialyltransferase revealed a similar positioning of donor, acceptor, and catalytic residues that provide a common structural framework for catalysis by the mammalian and bacterial sialyltransferases.
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