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. 2023 Sep 18;14:5785. doi: 10.1038/s41467-023-41238-1

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© The Author(s) 2023, corrected publication 2024

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — a View of the active sites of AaNGT-UDP-2F-Glc (upper-left panel), AaNGT-UDP-Gal (upper-right panel), and AaNGT-UDP-FGNWTT (lower-left panel) complexes. Residues are colored according to their location in the different domains and subdomains of AaNGT, with the same color scheme as used in Fig. 2a. The nucleotides UDP and the peptide are shown as gray and green carbon atoms, respectively. Hydrogen bond interactions are displayed as dotted black lines. b Superposition of the different ligands with UDP-Gal as yellow carbon/phosphate atoms, UDP-2F-Glc as orange carbon/phosphate atoms, UDP as gray carbon/phosphate atoms, and FGNWTT as green carbon atoms. c Glycosylation kinetics of AaNGT and mutants, measured against variable concentrations of the peptide FGNWTT and using a saturated concentration of UDP-Glc. Additional kinetic data are provided in Supplementary Table 1. All experiments were obtained in duplicate (n = 2 independent experiments). Source data are provided as a Source Data file.