Letter reSeArCH
Extended Data Fig. 2 | Comparison of Mgm1 and dynamin.
a, M onomers 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, C omparison between the stalk dimers of Mgm1 (left) and dynamin
(right). In both proteins, the dimer buries a total surface area of 1,200 Å^2.
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.