Extended Data Fig. 3: Intra- and inter-filament interactions.
From: Structural basis of mitochondrial receptor binding and constriction by DRP1
a, The triangular structure seen in cross section. Side 1 of the triangular structure has the atomic model placed in the density. The G-domain-to-G-domain contact between adjacent sides is circled. b, The sum of the three sides with the model fit in density. c, Ribbon diagram of the same atomic model as in b. The rotated view shows eight chains each of DRP1 and MID49. The chains further from the reader are rendered transparent. d, An isolated tetramer of DRP1 from the filament, rendered to highlight the stalk interfaces 1, 2 and 3 observed for DRP1 and other GTPases of the dynamin family. e, Expanded view of the circular region in a illustrating a salt bridge between adjacent G domains. f–i, Negative-stain micrographs of: DRP1-only wild-type polymers incubated with GMPPCP (f), DRP1 co-assembly with wild-type MID49(126–454) and GMPPCP (g; inset, high-magnification view), DRP1(E116R) mutant polymers (h), DRP1(E116R) mutant co-assembly with MiD49(126–454) (i). Shorter, single-sided filaments predominate. Disordered ‘triangular assemblies’ were also observed, but were much shorter and infrequent compared with the wild-type proteins. Scale bars, 50 nm.
