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. 2018 May 2;9:1773. doi: 10.1038/s41467-018-04137-4

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© The Author(s) 2018

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 — Recognition mechanisms and functional importance of the FlhA ternary complexes. a Superposition of the two ternary complexes (FlhA^C−FliT−FliD^C and FlhA^C−FliS−FliC^C) on FlhA^C. For clarity only the recognition helices are shown (FliT helix α4 and FliS helix α1). The two key residues recognized by FlhA is a Tyr (Tyr106 in FliT and Tyr10 in FliS) and a hydrophobic one (Leu102 in FliT and Ile7 in FliS). Sequence conservation of the recognition helices in FliT and FliS is also shown. b Effect of amino acid substitutions at the binding interface on the kinetics of bacterial motility. Bar graphs represent the mean value of the colony diameter and error bars represent standard deviation (n = 6)