Figure 7

G-BSE angle is larger in mutant dynamins. (A) Representation of the interaction region between the residue R/W465 and the BSE of the adjacent dynamin-2. G-domain is in blue, BSE is in yellow, stalk is in red, residue 465 is shown in purple, whereas the residues of the BSE P294, S298, S742, V744, and S745 are in lime. (A′) BSE residues that interact with R465 in the WT monomers of the WT and HT helices. (A″) BSE residues that interact with W465 in the mutant monomers of the HT and FM helices. In blue are highlighted the residues with higher occupancy, whereas the residue with low occupancy are in red. (B) Plot of the area of interaction between the residue 465 and the BSE over the last 500 ns of simulation. (C) Scheme depicting the G-BSE angle. This angle is formed by the intersection of vectors V1 and V2, which correspond to the center of mass of residues 291–293. V1 ends at the center of mass of residues 277–285 segment while V2 at the center of mass of residues 299–306 segment. (D) Violin plot of G-BSE angles of the 56 monomers of WT and FM helices and 28 WT or mutant monomers of the HT helix (HT.WT and HT.MUT respectively). (E) Scheme depicting BSE-stalk angle. The BSE-stalk corresponds to the angle form by the intersection of vectors V3 and V4, which correspond to the center of mass of residues 315–321 and 702–711. Vector V3 ended at the center of the G-domain defined by segments 30–36 and 170–176. Vector V4 ended at the center of mass of residues 410–422 and 610–626. (F) Violin plot of BSE-stalk angles of the 56 monomers of WT and FM helices and 28 WT or mutant monomers of the HT helix (HT.WT and HT.MUT respectively). In D and F boxes indicate 25–75 percentiles, horizontal lines within boxes indicate medians, and whiskers indicate minimum and maximum angle values. ***p < 0.001 compared with WT or HT.WT (Kruskal–Wallis and Dunn’s multiple comparisons test). G domain is in blue, BSE is in yellow, stalk is in red, PH domain is in green.