Extended Data Fig. 2: Comparison of Mgm1 and dynamin.
From: Structure and assembly of the mitochondrial membrane remodelling GTPase Mgm1
a, Monomers of Mgm1 (left) and dynamin (right) coloured by domain. b, The G domain and BSE domain of nucleotide-free Mgm1 and dynamin (grey, PDB: 5A3F) were superimposed on the BSE domains with a Cα root-mean-square deviation (r.m.s.d.) of 2.6 Å and 40% sequence identity. Both structures are in the closed state. The nucleotide-binding site is indicated. c, Superposition of the upper part of the stalk between Mgm1 and dynamin. In contrast to dynamin, the stalk in Mgm1 is kinked. d, Comparison between the stalk dimers of Mgm1 (left) and dynamin (right). In both proteins, the dimer buries a total surface area of 1,200 Å2. However, in Mgm1, interface-2 is shifted towards the paddle, resulting in a V-shaped dimer, whereas the dynamin dimer is X-shaped. e, Association of two dimers in the respective tetrameric crystal structures. In dynamin, the assembly of dimers occurs via two interfaces (interface-1 and interface-3), whereas only interface-1 is present in Mgm1.
