Structure of the month

Figure 1. 

Dynamin (ΔPRD) has a four-domain architecture, composed of the G domain, the bundle signalling element (BSE), the stalk and the PH domain. Assembly via the central interface (crystallographic 2-fold axes, dotted line) leads to an extended dynamin dimer.

Figure 2. 

Model of oligomerized dynamin in the constricted state. G domains, BSEs, stalks and PH domains were fitted into a cryo-EM map (Mears, J. A. et al. Structure 15, 1190–1202 (2007)). Three dimeric building blocks are colored uniformly in yellow, blue and gray to show the spread of the 260 Å long dynamin dimer over 95° of a dynamin turn as well as the interaction of two neighboring turns via G domain - G domain contacts. Whereas thirteen stalk dimers complete one turn, the G domain of dimer (i) associates with the G domain of dimer (i+10).

Figure 3. 

Dynamin forms helical oligomers around membrane templates, such as necks of clathrin-coated vesicles. GTP binding and hydrolysis induce intra- and intermolecular domain rearrangements in the oligomer inducing a break of the underlying membrane template.