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. 2020 Jun 2;10:9002. doi: 10.1038/s41598-020-66050-5

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© The Author(s) 2020

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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VtrA and ToxR periplasmic domains are structural homologs. (a) Shows topological graphs of the ToxR and VtrA periplasmic domains generated by Pro-origami. The graph secondary structure elements are colored from N-terminal (blue) to C-terminal (red). The shaded area is the core domain as determined by Pro-origami. While Pro-origami assigned some of the loop regions in ToxR as helices (circled) and α1 in ToxR was broken into two helices (rectangle) the two structures share the same topology. (b) Overlay of the VtrA structure, (5kev) (orange) and the Vv-dbToxRp structure (blue). A single arrow points to the VtrA terminal helix, (middle panel) and a double arrow shows the displacement of the last strand between the VtrA and ToxR (middle panel). The cysteine sulfur atoms are shown as yellow spheres for clarity.