Figure 1 Model of FATP synthase dimer viewed

Figure 1. Model of F-ATP synthase dimer viewed from the lateral side ( A) and from the intermembrane space (B). A: left monomer, the F 1 and FO sectors are highlighted. Right monomer, the F 1 and FO subunits are shown. In the F 1 sector, the front α and β subunits have been removed to reveal the central stalk. The F 1 α and β subunits are colored in red and yellow, respectively. The F 1 γ, δ, and ε subunits are colored in shades of blue, the peripheral stalk subunits b, d, F 6 and OSCP in shades of green, and the c-ring in purple. The remaining FO subunits a, e, f, g, and A 6 L are colored in light blue. The intramembrane FO is surrounded by detergent, shown in white. The image has been built starting from the yeast dimer molecular model (146) (PDB id. 4 b 2 q) to which the cryoelectron microscopy (cryo-EM) map of bovine F-ATP synthase (29) (EMD id. EMD-2091) has been superimposed. The fit of molecular models to cryo-EM map was performed using the program ADP_EM (208). The molecular model for bovine F-ATP synthase was obtained by superimposing the 3 D structure of the bovine F 1 -c-ring complex (PDB id. 2 xnd) onto each corresponding monomer of the yeast dimer. The superposition was performed using the Swiss pdb viewer routine Iterative magic fit (237). The lateral stalk was taken from the yeast dimer (PDB id. 4 b 2 q) which has been modeled using the bovine subunits. B: cryo-EM maps are rotated 180° to be viewed from the intermembrane space. DOI: (10. 1152/physrev. 00001. 2015)