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. 2021 Sep 13;17(10):1075–1083. doi: 10.1038/s41589-021-00858-8

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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. 2 — a, Structure of ARIH2* complex with neddylated CUL5 (spanning from CR3 domain to C terminus)-RBX2 is shown with domains colored as in Fig. 1. Black arrow indicates the >30 Å distance between the ARIH2* UBAL domain and NEDD8. Zinc atoms as spheres, and Ariadne domain helices numbered. b, Structural transition of CUL5 H29-helix and WHB domain between the unneddylated CUL5-RBX2 and neddylated CRL5^Vif-CBFβ-A3C-ARIH2* complex (ARIH2* and RBX2 RING domain are not shown for simplification). To visualize the relative position of the unneddylated CUL5 H29-helix and WHB domain (dark green), the region encompassing the CR3, 4HB and C/R domains from unneddylated CUL5-RBX2 (ref. ²²) was superimposed on the neddylated CUL5-RBX2-ARIH2* structure, but is not shown for simplification. In unneddylated CUL5, the H29-helix encompasses residues 697–725, whereas the first turn is unfolded and the H29-helix encompasses residues 700–725 in neddylated CUL5. c, Close-up of interactions surrounding the covalent isopeptide linkage between NEDD8 (yellow) and CUL5 H29-helix portion of the WHB domain (dark green). d, Three-way interface between NEDD8, its covalently linked CUL5 H29 helix and WHB domain, and a CUL5 surface from the C/R domain (relative to c, rotated 80° in x and 40° in y). e, ARIH2-catalyzed fluorescent UB (*UB) transfer to A3G in 10 min, mediated by WT unneddylated (no NEDD8), WT neddylated CRL5^Vif-CBFβ (WT) or versions with indicated mutations of CUL5 residues making noncovalent interactions with NEDD8. N = 2 independent experiments. For samples from same experiment, gels were processed in parallel (Source Data Fig. 2).

Source data