Fig. 2: Cryo-EM structures of native Otu2-40S complexes.
From: Molecular basis for recognition and deubiquitination of 40S ribosomes by Otu2
a, b Cryo-EM density maps (top) and molecular models (bottom) of the Otu2-bound and eS7 monoubiquitinated 43S-PIC complex (a) and 48S-IC (b). c, d Cryo-EM density maps (left) and molecular models (right) of the Otu2-bound late pre-40S complex (unmodified eS7) and the in vitro reconstituted Otu2-Ub-40S complex (d). In d, only the model for the 40S body is shown and the 40S head is displayed as transparent density. The map in (d) is displayed as composite map after multi-body refinement (see Supplementary Figs. 3a and 5) and low-pass filtered according to local resolution (see Supplementary Fig. 5). TC ternary complex consisting of trimeric eIF2αβγ complex, initiator methionyl tRNA (tRNAi) and GTP; ISS intersubunit surface, SS solvent surface, hd head, bk beak, pl platform, rf right foot, lf left foot, Ub ubiquitin. e Schematic illustration of Otu2 secondary structure and domains. Structurally visible parts are highlighted as orange boxes and interaction sites with the 40S are indicated.
