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. 2021 Feb 3;590(7847):671–676. doi: 10.1038/s41586-021-03197-9

Fig. 3. ARIH1 ubiquitylation of a range of substrates recruited to diverse F-box proteins.

Fig. 3

a, Structure representing TS2: ubiquitin transfer from ARIH1 to SCF substrate. The Ub-guided helix of ARIH1 and ensuing Rcat domain bound to ubiquitin form a ubiquitin transferase module barricaded by the switch helix of ARIH1. b, Approximately 100° reorientation of ubiquitin transferase module (shown in surface) between TS1 (light pink and melon) and TS2 (dark pink and orange), shown by aligning CUL1–RBX1 and the E3–E3act super-domain of the two transition state structures. Yellow star denotes the catalytic cysteine of ARIH1. c, Cartoon representations of various F-box proteins (grey) and their substrates (red) relative to zones accessible to ubiquitin-linked active sites of ARIH1 (pink) and UBE2D (cyan), based on structural modelling. K, substrate lysine. d, Graphs showing the mean value of catalytic efficiencies (kobs/Km) for ARIH1 (pink)- and UBE2D3 (cyan)-mediated ubiquitylation with indicated substrate and F-box protein, as depicted in c. n = 3 independent experiments.