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. 2020 Aug 28;11:4321. doi: 10.1038/s41467-020-18063-x

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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. 1 — a The Rc-cellulosomal network is assembled through interactions between Doc and Coh domains. Cellulose-binding domains, digestive enzymes, and structural scaffold proteins (Sca) self-assemble into a cellulosome complex, which binds and digests cellulose fibers in the human gut. XMod-DocB and CohE form a mechanically stable protein complex that anchors the cellulosomal network to the cell surface. b, c Structural models showing the XMod-Doc:Coh complex in the two hypothesized-binding modes. Green: Coh, blue: Doc, purple: XMod. Calcium ions are shown as black spheres. In both binding modes, the rupture forces observed for the five most stable models were measured by performing 200 steered molecular dynamics (SMD) replicas and plotting as histograms. The pulling directions are marked by black arrows. Rupture force histograms were fitted with Gaussian distributions. The most probable rupture force was 981 pN in binding mode A (panel b) and 575 pN in binding mode B (panel c) at a pulling speed of 5.0 Å ns⁻¹.