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. 2022 Feb 14;13:850. doi: 10.1038/s41467-022-28511-5

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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. 1 — a Cryo-EM density of FLYC1 colored by subunit and enclosed in detergent micelle (unsharpened map gaussian-filtered to 1.5 σ). Side (b) and top (c) view of FLYC1 model. In top view, TM helices are labeled from 1 to 6, according to their position in the amino acid sequence. d Cartoon representation of protomers of EcMscS (PDB: 2OAU, closed state), FLYC1, and AtMSL1 (PDB: 6VXM, closed state). e Side views of FLYC1 heptamer and its homologs, with two protomers colored blue and pink, respectively. Rotation of TM helices of each protomer relative to conserved cytoplasmic cage is limited for FLYC1 relative to AtMSL1 and EcMscS, where TM helices interact with cytoplasmic domain of the contiguous subunit. TM1–TM2 of FLYC1 are not shown for simplicity.