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. 2019 Aug 2;9:11216. doi: 10.1038/s41598-019-46038-6

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© The Author(s) 2019

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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A mechanochemical model for the flagellar motor. Interaction of the cytoplasmic loop in PomA with FliG induces sliding motions of TM-3 and TM-4 toward cytoplasmic side (A). This rearrangement approaches T158 in TM-3 toward D24 in TM-B and forms Na⁺ binding site by three modes of interaction (B). After release of the Na⁺ into the cytoplasmic side, TM-3 and TM-4 return to the original position. This re-sliding motion induces a conformational change in the cytoplasmic loop to produce torque at the interface with FliG (C).