Fig. 1: Cryo-EM and CG-MD structures of membrane deformations induced by CHMP1B and IST1.
From: Brominated lipid probes expose structural asymmetries in constricted membranes
a,b, Gray-scale top-down (a) and side views (b) of central slices of the cryo-EM density for the CHMP1B–IST1 copolymer bound to a cylindrical lipid bilayer comprising the lipids shown in composition no. 1, Table 1. c,d, Top-down (c) and side views (d) of an equilibrated tubule within the protein coat from CG-MD simulations, in all-atom representation. CHMP1B in green, IST1 in cyan, cholesterol in light gray, lipid tails in dark gray, phospholipid glycerol moieties in salmon, phospholipid phosphates in orange, SDPC headgroups in beige, POPS headgroups in yellow and PIP2 headgroups in pink. See PDB 6TZ5 for the protein structure. e, Side view of the lipid bilayer nanotube’s cryo-EM density with protein masked. f, Side view of the simulated CG-MD membrane tubule with protein hidden shows two bands where headgroups are displaced, and lipid tails are exposed. Color scheme is the same as in c and d. g, EM density of the outer leaflet of the bilayer visualized in cylindrical coordinates. The periodic footprint of CHMP1B is apparent at this depth. h, Normalized two-dimensional headgroup density of outer leaflet phospholipids from CG-MD simulations (headgroup exclusion zone appears as dark low-density bands) with F9 and F13 side chain locations (green dots). Data for graphs in g and h are available as source data.
