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. 2021 Jul 14;12:4322. doi: 10.1038/s41467-021-24554-2

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© The Author(s) 2021

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. 3 — a Multiple sequence alignment of the region surrounding residues F125 and F128 (marked with asterisks) in securin orthologs. b The molecular surface of separase (green) in contact with the region of securin detailed in Fig. 3a (purple). Image generated using the crystal structure of the Saccharomyces cerevisiae separase-securin complex (PDB accession 5U1T [10.2210/pdb5U1T/pdb])¹⁸. The side chains of securin residues Y276 and F279, which correspond to F125 and F128 in the human protein, are shown as stick models and labelled in purple. The N- and C-termini of the securin segment displayed are also labelled in purple c Schematic representation of a tethered separase-securin complex reporter (separase-securin FL) including a cartoon demonstrating predicted complex interaction. d Mean VFP-tagged securin FL (magenta trace, n = 8) and separase-securin FL (green trace, n = 6) destruction profiles relative to PB1 extrusion.