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. 2021 Sep 23;28(10):799–810. doi: 10.1038/s41594-021-00656-9

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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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Extended Data Fig. 9 — (a-c) The α-Linker moves its docking site on β-Ring from Groove-1 in MTBS-1 (a) to Groove-2 in MTBS-2 (c), which is consistent with the groove where β-Linker docks on γ-Ring in MTBS-1 (b). (d) A comparison between OAD-PF arrays in MTBS-1and MTBS-2 from three different views. Each array is generated by elongating the identical 48-nm OAD-PF maps in the same MTBS. (e-f) Cryo-EM reconstruction of the reconstituted OAD arrays (left) and the corresponding states from our cryo-ET analysis (right). The slices are focused on β-HC to show the key difference between MTBS-1 (e) and MTBS-2 (f). The single particle reconstructions were generated by joining two identical 48-nm OAD-PF maps. The cryo-ET maps were generated by sub-volume averaging from two representative tomograms. (g-h) The OAD arrays in MTBS-1 and MTBS-2 are assembled in the same TTH manner. The TTH interfaces are marked by the dashed black circles. (i-j) Substituting one OAD unit in MTBS-1 (i) with a unit in MTBS-2 (j) severely disrupts the interactions between the IC-NDD₀ and the α/β₊₁-LR region (j, right).