Fig. 3: Analysis of the Hinge conformations.

a The GG dimers in the one-start and the two-start helix. The one-start helical strand is colored gray, and the two two-start helical strands are colored in green and orange, respectively. The GG dimers circled are used for structural analysis and monomers from them are colored accordingly through (b) to (h). b, c Structural comparisons of the two asymmetric monomers between the two helical symmetries. Monomers with similar Hinge 2 conformations between the one-start and the two-start helix are aligned based on the Stalk domains. 1.8° (b) and 4.2° (c) rotations around Hinde 1 are observed. d Flexibility of the Hinge 1 conformation. The Stalk domains are aligned between the two monomers from the two-start helix and the crystal structure (colored in purple, PDB: 5A3F). e Conformations of Hinge 2 of the two monomers from the two-start dynamin helix. One monomer (colored in orange) has a kink centered around T292 and P294, which in the other (colored in green) is a continuous helix. The GTPase domain swings 46° around Hinge 2 between the two monomers when the BSE domains are aligned. f Flexibility of Hinge 2 conformation. The GTPase domains are aligned between the two monomers from the two-start helix and the crystal structure (colored in magenta, PDB: 3SNH). g, h Hinge 1 alters the Stalk orientation within the GG dimer. The GTPase domains are aligned in (g) and the Stalk domains of the bottom molecule are aligned in (h). Red arrows indicate the domain movements, black dashed arrows indicate the Hinge 2 locations, the blue dashed arrows indicate the Hinge 1 locations, and black dashed lines indicate the GG dimeric interface. i Color code of the dynamin monomers.