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. 2021 Nov 11;12:6508. doi: 10.1038/s41467-021-26796-6

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© The Author(s) 2021

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. 6 — a Superimposition of OGT structures (polypeptide backbone only) onto OGT/UDP (PDB: 3PE3, left) and the position adopted in TPR10 of proteins within the space group (right)^{9, 13, 35–37}. No difference in the catalytic regions are observed, while TPR 10 is susceptible to crystal packing due to a high degree of flexibility. b In the OGT/UDP-5SGlcNAc/LaminB1 peptide ternary complex (SG: F222, PDB: 5BNW, blue) the peptide (purple) does not interact with the TPRs, however, TPR 10 is shifted in relation to OGT/UDP structure (SG: P321, pink)²⁷. The OGT/UDP/gTAB1 ternary peptide structure (SG: P321, PDB: 4AY5, green) shows the peptide (purple) extending into TPR units and TPR 10 is identical compared to the OGT/UDP structure (SG: P321, pink)²⁸.