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. 2023 Jan 5;299(2):102869. doi: 10.1016/j.jbc.2023.102869

Figure 4.

Figure 4

Dynamic oligomerization and conformational flexibility of Armc8β.A, SEC–MALS analysis of the Armc8β self-association (similar to Fig. 2B). B, blue native PAGE analysis of Armc8β. C, the crystal structure of Armc8β (PDB entry: 8A1I) reveals three chains in the asymmetric unit: chains p (green), i (gray), and a (black). D, overlay of the three chains in ribbon representation reveals conformational changes. Rms deviations of the different chains toward each other are summarized in the bar chart. E, comparison of the p chain (ribbon) of Armc8β with Armc8α as observed in the cryo-EM structure of the RTα–Gid4 complex (PDB entry: 7NSC). Superposition of the three different chains of Armc8β with Armc8α (purple) in ribbon representation illustrates the rms deviations depicted in the bar chart. F, model of how complex binding rigidifies the flexibility of Armc8. SEC-MALS, multiangle light scattering coupled to analytical size-exclusion chromatography; PDB, Protein Data Bank.