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. 2022 Jul 19;5:695. doi: 10.1038/s42003-022-03661-w

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© The Author(s) 2022

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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — a Purity of the GnT-IVa lectin domain and its D445A mutant prepared from E. coli was checked by SDS-PAGE and subsequent CBB staining. b Elution profiles of the gel filtration analysis during the purification step are shown. Protein absorbance (A₂₈₀) and ion conductance were colored in blue and red, respectively. The peak of ion conductance indicates the point of one column volume. c Overall structure of the lectin domain of mouse GnT-IVa D445A. d Structural neighbors of GnT-IVa lectin domain defined by DALI. Overall structures of NagH (PDB code: 2W1U³⁰, left panel) and IFT25 (PDB code: 2YC4³¹, right panel), which are structurally similar proteins to the GnT-IVa lectin domain. These two proteins are viewed from the same angle as c. The carbohydrate and calcium ion are shown in stick and sphere models, respectively. e Close-up view of putative sugar binding sites of GnT-IVa (blue, left panel) and the corresponding regions of NagH CBM32 in complex with GlcNAcβ1-3GalNAc (PDB code: 2W1U, grey, middle panel) and IFT25 (PDB code: 2YC4, right panel). Four corresponding residues are shown in stick models and labeled.