Fig. 6

MD simulations reveal a closed anion permeation pathway. a Averaged water densities in absence or presence of the hydrocarbon chain along the central axis from unguided MD simulations contoured at 1.2σ in side view. Helices A and B of three subunits are shown in cartoon representation and pore-lining residues as sticks. b Na⁺ (blue) and Cl⁻ (red) densities for WT and F24A-L28A mutant proteins in absence of the detergent contoured at 0.2σ. c Pore radii along the pore axis (positions relative to the protein center of mass) for the conformational ensemble sampled in WT simulations without hydrocarbon chain. Side chain positions of residues Phe24, Leu28, and Arg29 are shown. d Electrostatic potential distribution calculated from the MD simulations mapped onto the solvent-accessible surface of OLPVRII in side view. The two front subunits are hidden for clarity. e Potential of mean force profiles for water, Na⁺, and Cl⁻ permeation along the pore. f Histograms of the number of water molecules observed within the hydrophobic gate region for different mutations. Source data are provided as a Source Data file