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. 2024 Feb 21;627(8003):437–444. doi: 10.1038/s41586-024-07093-w

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© The Author(s) 2024

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — a, View of the catalytic region of the UREL complex bound to the 60S ribosome showing the UFBP1 UFIM and CDK5RAP3 N terminus bound to UFM1. The distance between the C termini of UFM1 and RPL26 in our cryo-EM model is shown as a black dashed line. Missing residues of UFM1 and RPL26 are shown as dashed lines in their respective colours. b, 3DFlex was used to generate motion models of the UREL ligase complex. The black arrows indicate the direction of motion observed. c, AlphaFold prediction of the UFBP1 UFIM–UFM1 complex. Inset: an enlarged view of the UFBP1 β1 and UFM1 β2 interface; key interactions are highlighted. d, Cryo-EM density map of UFMylated 60S ribosomes shown in transparent grey with a model of UREL ligase bound to 60S rigid-body fitted into the density.