ArticleThe Journal of biological chemistry2013
Crystal structures of β-1,4-galactosyltransferase 7 enzyme reveal conformational changes and substrate binding.
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 31 papers.
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Who cites it
31 citing papers in PubMed, 53 citations in OpenAlex.
- Structural basis of chondroitin sulfate backbone polymer synthesis.Nature communications · 2026Article
- Xylosyltransferase engineering to manipulate proteoglycans in mammalian cells.Nature chemical biology · 2026Article
- Human Proteoglycan Linkage Region Glycosyltransferases are Dimeric and Show Unexpected Specificities.Angewandte Chemie (International ed. in English) · 2026Article
- Design of Glycosyltransferase Inhibitors: Targeting the Biosynthesis of Glycosaminoglycans by Phosphonate-Xyloside.ACS omega · 2025Article
- Structural basis for human chondroitin sulfate chain polymerization.Nature communications · 2025Article
- Synthesis, conformational analysis and biological activity of xylopyranosyl sulfur-containing glycosides: dependence of sulfur atom configuration.RSC advances · 2025Article
- Article
- Molecular Mechanisms Underlying the Loop-Closing Dynamics of β-1,4 Galactosyltransferase 1.Journal of chemical information and modeling · 2025Article
- Glycosyltransferases: glycoengineers in human milk oligosaccharide synthesis and manufacturing.Frontiers in molecular biosciences · 2025Review
- Genetic variability in proteoglycan biosynthetic genes reveals new facets of heparan sulfate diversity.Essays in biochemistry · 2024Review
- The Transpeptidase Sortase A Binds Nucleic Acids and Mediates Mammalian Cell Labeling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Chemo-enzymatic synthesis of tetrasaccharide linker peptides to study the divergent step in glycosaminoglycan biosynthesis.Glycobiology · 2024Article
- Structural and mechanistic characterization of bifunctional heparan sulfate N-deacetylase-N-sulfotransferase 1.Nature communications · 2024Article
- Molecular mechanism of decision-making in glycosaminoglycan biosynthesis.Nature communications · 2023Article
- Structural and biochemical insight into a modular β-1,4-galactan synthase in plants.Nature plants · 2023Article
- Fluorescently labeled xylosides offer insight into the biosynthetic pathways of glycosaminoglycans.RSC advances · 2021Article
- Exploration of human xylosyltransferase for chemoenzymatic synthesis of proteoglycan linkage region.Organic & biomolecular chemistry · 2021Article
- Chemoenzymatic Synthesis of Glycopeptides Bearing Galactose-Xylose Disaccharide from the Proteoglycan Linkage Region.Organic letters · 2021Article
- Synthesis and Screening of α-Xylosides in Human Glioblastoma Cells.Molecular pharmaceutics · 2021Article
- Recent advances on glycosyltransferases involved in the biosynthesis of the proteoglycan linkage region.Advances in carbohydrate chemistry and biochemistry · 2021Review
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3 authors at 2 institutions in 1 country.
Funding
Abstract
The β-1,4-galactosyltransferase 7 (β4GalT7) enzyme is involved in proteoglycan synthesis. In the presence of a manganese ion, it transfers galactose from UDP-galactose to xylose on a proteoglycan acceptor substrate. We present here the crystal structures of human β4GalT7 in open and closed conformations. A comparison of these crystal structures shows that, upon manganese and UDP or UDP-Gal binding, the enzyme undergoes conformational changes involving a small and a long loop. We also present the crystal structures of Drosophila wild-type β4GalT7 and D211N β4GalT7 mutant enzymes in the closed conformation in the presence of the acceptor substrate xylobiose and the donor substrate UDP-Gal, respectively. To understand the catalytic mechanism, we have crystallized the ternary complex of D211N β4GalT7 mutant enzyme in the presence of manganese with the donor and the acceptor substrates together in the same crystal structure. The galactose moiety of the bound UDP-Gal molecule forms seven hydrogen bonds with the protein molecule. The nonreducing end of the xylose moiety of xylobiose binds to the hydrophobic acceptor sugar binding pocket created by the conformational changes, whereas its extended xylose moiety forms hydrophobic interactions with a Tyr residue. In the ternary complex crystal structure, the nucleophile O4 oxygen atom of the xylose molecule is found in close proximity to the C1 and O5 atoms of the galactose moiety. This is the first time that a Michaelis complex of a glycosyltransferase has been described, and it clearly suggests an SN2 type catalytic mechanism for the β4GalT7 enzyme.
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