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Figure 1
(a) CryoEM map of Yarrowia lipolytica complex III dimer. The consensus map (EMD-15312) of the complex at an overall resolution of 2 Å is shown. The map was calculated with deepEMhancer (Sanchez-Garcia et al., 2021BB4) from the two half-maps. The core subunits of complex III, cytochrome b, c1 and ISP are coloured orange, green and purple, respectively. The supernumerary subunits are coloured in tan and the non-protein densities are in black. Unmodelled densities are shown in grey, in particular the blurred density of the ISP hydro­philic domain can be seen. (b) The surface representation of the consensus model (PDB entry 8ab6) of complex III is shown in white. The co-factors and lipid/detergent molecules are shown in stick representation (the carbon atoms in heme bL and heme bH in purple, high potential heme c1 in blue, and lipid/detergent molecules in green). The water molecules are shown as red spheres. In the consensus model, only the transmembrane helix of the Rieske protein has been modelled and hence the 2Fe–2S cluster is not shown. (c) The surface representation of the core subunits of complex III with the TM helix of ISP coloured in purple. Typically observed positions of the hydro­philic domain of ISP are shown (from antimycin-treated samples) from b position to c position (blue, green and red for b, intermediate and c positions, respectively, are shown in cartoon representation). The 2Fe–2S cluster is shown as spheres and the movement of this cluster is shown with an arrow. The quinones in the Qi site (green) and the Qo site (cyan) are from different models (PDB entries 8abk and 8ab8, respectively) but shown in this figure to highlight the quinone binding sites. Figures were prepared with Chimera (Goddard et al., 2007BB91) and PyMOL (DeLano, 2002BB90).

IUCrJ
Volume 10| Part 1| January 2023| Pages 1-3
ISSN: 2052-2525
https://doi.org/10.1107/S2052252522012003