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. 2021 Jun 29;12:3889. doi: 10.1038/s41467-021-24151-3

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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. 6 — a Conformational changes of TM11/TM12 in the transmembrane domain of the T protomer induced by drug binding (yellow, unliganded T; cyan, partially induced T in presence of β-lactams; green, partially induced T of 3-FOR bound Gly619Pro; magenta, fully induced T in presence of fusidic acid (FUA) bound to the TMD-BP. b FUA (carbon, black; oxygen, red) binding to TMD-BP of the T protomer (yellow). Inset: Polder electron density map assigned to FUA is contoured at 4.5 σ. c Substrate protection experiment of AcrB-cl_Cys981 and AcrB-cl_Cys875 (negative control) by in-gel fluorescence of MTS-rhodamine modified proteins in dependence of the drug concentration (from left to right increasing concentration of drugs). Data are presented as mean ± s.e.m. of N ≥ 4 independent experiments. The calculated apparent K_i^app for fusidic acid, oxacillin, or novobiocin is 38, 446, or 95 μM, respectively (Source Data Fig. 6c).