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. 2020 Apr 14;11:1774. doi: 10.1038/s41467-020-15645-7

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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 Domain architecture of MavC showing interaction modes among MavC, UBE2N, and Ub. b Overall structure of the MavC/UBE2N/Ub complex, colored as in a. Q40 of Ub, K92 and K94 of UBE2N are shown as sticks. c Overview of the interfaces between MavC and Ub in the MavC/UBE2N/Ub complex. d Overall structure of the MavC/UBE2N/Ub complex, with Ub shown in the electrostatic surface model. e–g Detailed interfaces of MavC–Ub interaction as marked in c, including A1 e, B1 f and C1 g. Hydrogen bonds are represented as red dashed lines. h Detailed CTC interface of MavC–Ub interaction as marked in c. Ub in the CHBP/Ub structure is colored in blue, and aligned to that in the MavC/UBE2N/Ub complex. i Mutations of the MavC-interacting residues in Ub decreased its ability in MavC-catalyzed ubiquitination. Ub and its mutants were incubated with MavC and UBE2N for 1 h at 37 °C. Then the samples were subjected to Tricine gel, followed by Coomassie blue staining. Source data are provided as a Source Data file. The experiment was repeated independently three times with similar results.