Fig. 6

The lid of Osh6p prevents the protein from binding to PS-rich membranes. a Electrostatic features of the molecular surface of Osh6pΔ35 and Osh6pΔ69. b Co-evolution of the height and orientation of the protein relative to the membrane surface during each trajectory. The height is calculated between the mass center of Osh6pΔ35 (residue 35–434, trace Δ35–1 to-4) or Osh6pΔ69 (residue 70–434, trace Δ69-1 to 4) and the plane of the DOPC/POPS bilayer during each 500 ns simulation. The orientation is given by the angle between the 346–356 segment of the α7 helix and the plane of the membrane. The time evolution is shown with colors going from blue (beginning of the MD trajectory) to green (end of the trajectory). Dark circles and triangles correspond to the distance and angle values associated to the initial and final configuration (t = 500 ns) of each protein, respectively. c Configuration of Osh6pΔ35 and Osh6pΔ69, bound to the surface of the lipid bilayer at 300 ns of the Δ35-1 trajectory and at the end of the Δ69-2 trajectory, respectively. The surface of the protein is shown except for residues of the β11-β12, β14-β15, and β17-β18 loops, which are in contact with the membrane: the atoms are represented as sphere with carbon in orange, oxygen in red, nitrogen in blue and hydrogen in gray. The lid with the D/E-rich motif is drawn in a ribbon mode. The molecule of POPS inside the binding cavity of Osh6pΔ35 is represented in a stick mode. Lipids of the membrane are shown in blue grey as stick. The walls of the binding site are colored in green. d Percentage of time Osh6p’s residues are in close contact with the membrane. The identities of loops and others structural elements that insert in the membrane, are indicated. Source data are provided as a Source Data file