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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. 2 — Structural properties of the export gate protein FlhA^C. a Cartoon rendering of the crystal structure of FlhA^C determined at 1.9 Å resolution. The protein is colored using a continuous-gradient color scheme from the N terminus (blue) to the C terminus (red). b Solvent-exposed surface rendering of FlhA^C displayed in the YRB color scheme⁵⁹ (yellow, carbons not attached to nitrogen or oxygen; red, negatively charged; blue, positively charged). c The FlhA^C site determined by NMR to interact with its binding partners is highlighted in pink. d Sequence conservation of FlhA^C colored according to residue identity conservation scores obtained by ConSurf⁶⁰. The binding site is the most conserved surface in FlhA^C