Fig. 3: Three hinge regions enable the conformational plasticity of PspA.
From: Structural plasticity of bacterial ESCRT-III protein PspA in higher-order assemblies
a, Model of a PspA + ATP monomer showing details of the density at the loop connecting α3 and α4 (α1, red; α2 + 3, violet; α4, blue; α5, cyan) b, Superimposed PspA + ATP monomer structures aligned on the hairpin between α1 and α2 + 3 and color-coded by increasing rod diameter (blue to red for increasing diameters). Hinges 1–3 and the corresponding displacement angle are indicated by opening angle symbols (black). c, Graph of PspA + ATP rod diameters over the distance between Cα 82 and Cα 187. d, Graph of PspA + ATP rod diameter against the displacement angle at Hinges 1–3. e, Bar plot of selected pair distances evaluated over all determined diameter assemblies. For a plot of all evolutionarily conserved residue pairs and a more detailed explanation, see Extended Data Fig. 3c. Color code for residue letters: green, charged; yellow, hydrophobic; pink, polar + uncharged; gray, special cases. Color code for boxes: α1, red; α2 + 3, violet; α4, blue; α5, cyan. f, Model of PspA + ATP monomer with evolutionarily conserved amino acid residues highlighted and colored according to the flexibility of their contacts (green, low flexibility (s.d. < 1); red, high flexibility (s.d. > 1)). g, Model of the PspA + ATP monomer with electrostatic surface coloring. Arrowheads show the start and end of the non-conserved hydrophobic groove.
