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. 2020 Oct 8;11:5080. doi: 10.1038/s41467-020-18866-y

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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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Fig. 2 — The structures of VcPilQ (this study, dark red), V. cholerae GspD (5WQ8) (green), E. coli K12 GspD (5WQ7) (blue), and S. typhimurium InvG (6DV3) (yellow) are compared^{55, 61}. The putative outer membrane location is depicted as a blue rectangle. The structures are shown as multimers (a) or monomers (b). c The multimer is shown in tan with one subunit colored. The putative outer membrane region is highlighted to show that VcPilQ (left, red) has a ~30 Å membrane spanning distance, while VcGspD, EcGspD, and StInvG have about a 24 Å membrane spanning distance. d Adaptive Poisson–Boltzmann solver was used to calculate the electrostatic potential calculation of each secretin in PyMol¹⁴². The inner cavity of each secretin is shown. The scale varies from −5 (red) to +5 (blue) in units of K_bT/e_c.