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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. 1 — a Cartoon representation of YscX (cyan) and YscY (red). YscX binds to YscY at two independent sites. b, c Surface hydrophobicity gradient of YscY shown from hydrophobic (red) to hydrophilic (white) using the normalized consensus hydrophobicity scale⁶⁵. b YscX binds the groove of the TPR protein YscY via the hydrophobic side of a short amphipathic helix. c Two leucine-rich helices of YscX interact with the largely hydrophobic surface of the N-terminal TPR in YscY. d Superposition of YscX₅₀:YscY (cyan and red) and YscX₃₂:YscY (blue and pink) models. The alignment was calculated using the Cα atoms of YscY. Zoom-in shows the YscX N-terminus before α1 for both structures when aligned using the Cα atoms of YscX.