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. 2020 Apr 30;10:7384. doi: 10.1038/s41598-020-64115-z

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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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Superimposition of the PorE OmpA_C-like domain structure with other representative OmpA family proteins (same as in Fig. 3). Structures of the proteins are displayed as a ribbon diagram with worm format; the peptidoglycan (PG) fragments as well as the three conserved residues whose side chain is involved in hydrogen bonds with the PG fragment are displayed in stick format, with nitrogen and oxygen atoms displayed in blue and red, respectively. The protein chains and their bound PG fragments are respectively shown in white and grey (PorE OmpA_C-like domain), yellow and orange (A. baumannii PAL, 4G4V), and blue and cyan (A. baumannii OmpA, 3TD5). V. alginolyticus PomB (3WPW), that contains no PG fragment, is shown in magenta. For clarity purpose, only the PorE OmpA_C-like domain residues are labelled, and the orientation is rotated 90° from Figs. 1 and 2 along the vertical axis. The figure was prepared using PyMOL (version 1.20, https://pymol.org).