Fig. 4: Comparison of the Stalk conformations between one-start and two-start Dyn1ΔPRD assemblies.

a–e Comparison of Dyn1ΔPRD Stalk tetramers from one-start and two-start assemblies (a), around the interface 3 (b, e), interface 2 (c), and interface 1 (d). The one-start tetramer is in gray and the two-start tetramer is colored. One Stalk domain (colored in cyan) from the two-start helix is aligned to its counterpart. The black arrows indicate the movements from one-start conformation to the two-start one. The detailed view of each interface is shown in Fig. S4. f The small motions within the Dyn1ΔPRD Stalk tetramer, which resulted in a small increase in the rise of individual assembly subunits (from 6.3 Å in one-start to 13.6 Å in two-start), propagates and accumulates through a helical turn. For clarity, only the Stalk domains of one rung are shown. The one-start is colored in light blue and the two-start is colored in orange. The putative location of the lipid bilayer is drawn in green dashed lines throughout the panels. Note, in panels (c) and (d), the membrane is located above and behind the page, respectively.