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. 2022 Jun 2;13:2858. doi: 10.1038/s41467-022-30487-1

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© The Author(s) 2022

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. 9 — YscV, YscX, and YscY are shown in orange, cyan, and red, respectively. a Superposition with the cryo-EM structure of YscV_C (gray, PDB: 7ALW), which is shown as cartoon representation. YscV_C protomers are aligned with an r.m.s.d. of 0.797 Å. b, c Superposition with FlhA (gray) bound to the flagellar chaperone:substrate complexes (green:light green). b FlhA:FliS:FliC (PDB: 6CH3). c FlhA:FliT:FliD (PDB: 6CH2). Alignments were obtained using SD3 of YscV_C (residues 514–600) with an r.m.s.d. of 1.194 Å (PDB: 6CH2) and 1.207 Å (PDB: 6CH3). d YscVXY superimposed with Chlamydia pneumoniae CdsV in complex with the stalk protein CdsO (PDB: 6WA9). The alignment was calculated using SD3 of YscV_C with an r.m.s.d. of 0.854 Å. Two subunits of YscV and CdsV (gray) are shown, CdsO is colored in green.