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. 2023 Jul 1;14:3896. doi: 10.1038/s41467-023-39678-w

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© The Author(s) 2023

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 Overall configuration of the BceS TM helices and HAMP domain. Each monomer of BceS is colored either red or yellow. Blue dashed lines indicate the approximate boundary of the lipid bilayer. b View from the extracellular space of the tip of BceS TM helices. The core of the TM helix bundle contains a cluster of sulfur containing side-chains and hydrogen bonds between two pairs of glutamines. c View from the extracellular space of the middle of the BceS TM helix bundle, showing that the core of the bundle in the membrane interior contains a network of π-stacking interactions between aromatic side-chains. d View of the BceS TM helix bundle near the interface of the membrane and cytosol. An electrostatic network of charged residues mediates interaction between BceS TM helices.