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. 2021 May 18;12:2927. doi: 10.1038/s41467-021-23248-z

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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. 2 — A cartoon structural model of RtMprF flippase domain viewed along the membrane plane (a) and from periplasmic side (b). The endogenous LysPG molecule associated with the flippase domain is highlighted as a sphere model in yellow. TM, transmembrane helix. c Topology of the flippase domain of RtMprF protein. The purple dashed boxes indicate the two motifs (Motifs 1 and 2) in Subdomain 1 with inverted topology. H1–H4, amphipathic helices 1–4. B1 and B2, β-strands 1 and 2. d Two major contact interfaces between the flippase domain and synthase domain of RtMprF. Color codes: cyan, synthase domain; magenta, flippase domain; yellow, LysPG. The dash boxes indicate the local regions of Interfaces 1 and 2 between the two domains. Zoom-in views of Interfaces 1 (e) and 2 (f) showing the specific interactions between adjacent amino acid residues from two neighboring domains. The numbers labeled nearby the dash lines are the distances (Å) between two adjacent groups.