Fig. 3: Molecular modelling of the human prohibitin complex.

a, A cartoon representation of the predicted structures of PHB1 (green) and PHB2 (white) molecules positioned into the final cryo-EM map (light grey, transparent) in side view (left) and top view (right), with (i) a complex consisting of six PHB1 and five PHB2 molecules and (ii) a complex consisting of five PHB1 and six PHB2 molecules. b, The surface representation (left) and interfaces of neighbouring prohibitin molecules (right) with the hydrophobicity surface. Orange colours represent hydrophobic side residues (i and ii); the hydrophobic transmembrane domains anchor prohibitins to the membrane (i), the top of the prohibitin complex is stabilized by the hydrophobic C-termini (ii) and the electrostatic potential surface (iii); blue indicates negatively charged side chains and red indicates positively charged side chains.