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. 2019 Nov 18;8:e51179. doi: 10.7554/eLife.51179

Figure 1. Structure of the E. gracilis ATP synthase dimer.

(A) Atomic model of the complete E. gracilis ATP synthase dimer with both subcomplexes in rotational state-1. The 2-MDa dimeric F1Fo-complex contains 29 different proteins. Dashed lines indicate C2-symmetry axis and 45° dimer angle. (B) OSCP/F1/c-ring subcomplex in rotational state-1, bound to its natural inhibitor protein IF1 (cyan), remaining Fo transparent. (C) Density map showing the lumen-exposed Fo region. Detergent belt shown in yellow; c-ring β-barrel in dark grey, Fo subunits as in (A). (D) Close-up of the lumenal interface of ATPEG1 (blue) with the c-ring (grey). The interaction occurs mostly via hydrophobic interactions (blue and grey sticks). (E–G) Euglenozoa-specific Fo-subunits with known folds. (E) ATPTB1 in blue superposed with Mdm38 (PDB ID: 3SKQ) (Lupo et al., 2011), six conserved helices coloured yellow, rest grey. (F) ATPTB3 in blue superposed with a bacterial homoisocitrate dehydrogenase in orange (PDB ID: 4YB4)(Takahashi et al., 2016), adopts a Rossman-fold. (G) ATPEG5 in yellow is a structurally conserved ortholog of the cytochrome c oxidase subunit VIb superfamily; bovine subunit VIb in purple (PDB ID: 2Y69) (Kaila et al., 2011).

Figure 1.

Figure 1—figure supplement 1. Cryo-EM data processing and classification scheme.

Figure 1—figure supplement 1.

(A) Representative micrograph. Scale bar 500 nm. (B) Representative 2D classes. (C) Fourier Shell Correlation (FSC) plots of all seven maps shown in D, with resolutions calculated according to the 0.143-cutoff criterion. (D) Cryo-EM data processing scheme. Final maps include the membrane region (from all rotational states), F1/c-ring maps from rotational states 1–3, the rotor and peripheral stalk tip (both from rotational state-1), as well as a consensus map of the ATP synthase dimer with both F1/c-ring subcomplexes in rotational state-1. Rotational state-3 displayed partial occupancy of IF1 and was separated into two classes with or without bound inhibitor using focused classification.
Figure 1—figure supplement 2. Local resolution estimation and model-map-correlations.

Figure 1—figure supplement 2.

(A–G) Density maps of masked regions of the ATP synthase coloured according to local resolution (left panels, local resolution as highlighted in color bars in Å) with Model-Map-FSC curves of respective atomic model refined into one half map to give FSCwork (black) and FSCtest (red)(right panels). (A) Membrane region, (B) consensus map of complete ATPS synthase dimer with both monomers in rotational state-1. (C–E) F1/c-ring maps of rotational states 1–3, (F) rotor in rotational state-1, (G) peripheral stalk tip of rotational state-1.