Extended Data Fig. 9: Characterization of the E1/E2 membrane helices and flexible hinge regions.
From: The hepatitis C virus envelope protein complex is a dimer of heterodimers
a, Cryo-EM map (transparent) overlayed with the predicted model of the different TM helices of E1 and E2. The helix positioned perpendicular to the C-terminal TM of E1, MX, is depicted in grey. b, Cryo-EM map showing the density of the E1/E2 homodimeric complex embedded in a detergent micelle. The left view is rotated 90 degrees compared to the right view. The micelle corresponds to the empty part of the volume, which is depicted in transparent grey. E1 is colored in steel blue and E2 is colored green. c-e, Comparison of flexible hinge regions, connecting the ectodomains to the TM helices, of our modeled structure (8rjj; depicted in light grey, top panel) with the recently solved E1/E2 heterodimer structure (7t6x; depicted in red, middle panel). The highlighted sections (dark grey) of E1 and E2 are aligned in a close-up view (bottom panel). c, Hinge regions connected to the internal TM helices of E1. d, Hinge regions connected to the C-terminal membrane-associated helices of E1. e, Hinge regions connected to the C-terminal TM helices of E2. Although the residue numbers differ between 8rjj (S52mod) and 7t6x (AMS0232) in the E2 alignment, the sequence in the highlighted section is highly conserved (e, bottom panel). The unresolved regions are indicated by broken lines.
