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. 2022 Aug 5;13:4399. doi: 10.1038/s41467-022-32019-3

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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. 2 — a Cryo-EM maps (upper) and ribbon models (lower) of M/Fab-E and M/Fab-B complexes. Unsharpened maps are shown in transparent light gray color (M/Fab-E complex: level = 0.08; M/Fab-B complex: level = 0.35), and B-factor-sharpened maps are show in multiple colors (M/Fab-E complex: level = 0.28; M/Fab-B complex: level = 0.75). M protein protomers, Fab-E, and Fab-B, are colored in purple, blue, green, and pink, respectively. b Structures of M protein dimer in the long form (upper) and the short form (lower) are shown from the side (left), front (middle), and bottom (right) views. One protomer of M protein is colored in a rainbow, and the other is light gray. Schematic views of the arrangement of six TM helices are shown on the lower right. TM1*, TM2, and TM3 formed one bundle. Throughout this paper, asterisks are used to indicate structural parts from the second M protein protomer. c Schematic view of the M protein protomer. Secondary structure elements and hinge regions are indicated. The disordered N-term and C-term regions are indicated by dashed lines. d Structure comparison between the long form (blue and cyan) and short form (orange and beige). The structures were aligned either according to the whole structure (left) or bundle A (right). e Detailed views of the interactions between the hinge region and bundle A in the long (upper) and short (lower) forms. The key residues are indicated in red. Dashed lines represent hydrogen bonds or salt bridges.