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. Author manuscript; available in PMC: 2016 May 22.
Published in final edited form as: Circ Res. 2015 May 22;116(11):1850–1862. doi: 10.1161/CIRCRESAHA.115.306557

Figure 1. Structure of bovine F-ATP synthase.

Figure 1

Left monomer, the F1 and Fo sectors are highlighted. Right monomer, the F1 and Fo subunits are shown. In the F1 sector the front α and β subunits have been removed to reveal the F1-rotor (central stalk). The F1 α and β subunits are colored in red and yellow, respectively. The F1-rotor γ, δ and ε subunits are colored in shades of blue, the peripheral stalk subunits b, d, F6 and OSCP in shades of green, and the c-ring in purple. The remaining Fo subunits a, e, f, g, A6L, whose structure has not been defined yet, are located in the Fo subcomplex colored in light blue. The image (lateral view) has been built starting from the yeast dimer molecular model133 (PDB id. 4b2q) and superimposing the cryo-electron microscopy map of bovine F-ATP synthase141 (EMD id. EMD-2091). The fit of molecular models to cryo-electron microscopy map was performed using the program ADP_EM198. The molecular model for bovine F-ATP synthase was obtained by superimposing the 3D structure of the bovine F1-c-ring complex (PDB id. 2xnd) onto each corresponding monomer of the yeast dimer. The superposition was performed using the swiss pdb viewer routine Iterative magic fit199. The lateral stalk was taken from the yeast dimer (PDB id. 4b2q) which contains the bovine subunits.