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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. 5 — Top view on the AcrB porter domain. Only the α-helical part of the PC1 and PC2 subdomains is shown (blue, L protomer; yellow, T protomer, red, O protomer). Binding of rifampicin-type (top row) and rifabutin/macrolide-type (bottom row) drugs to the access pocket (AP) is shown from left to right. The switch loop is colored in magenta. The dotted boundary of the ovals represents a closed deep binding pocket (DBP). Red arrow: the movement of switch loop. For further discussion on the mechanism see main text and Supplementary Note 2.5. PDB IDs of the displayed protomer structures: L, O: 4DX5; L^3-FOR: 6ZOB; L^ERY: 6ZOC; T^LIG1: 6ZO7; T^LIG2*, T^LIG3: 6ZO9.