Fig. 4
From: Structural basis for membrane tethering by a bacterial dynamin-like pair
Structural analysis of Cj-DLP1 bound to GDP·AlF4¯. a Cartoon of Cj-DLP1 monomer showing a BDLP1-like fold augmented with an N-terminal globular assembly domain (Cj-DLP1AD). Like BDLP1, Cj-DLP1 has a distinct highly flexible hinge 1 region. Here, hinge 1 and hinge 2 are in the open conformation. b G-domain superposition of Cj-DLP1α, Cj-DLP1β, and BDLP19. Hinge 1 facilitates a 125˚ in-plane rotation between symmetry mates. * = equivalent positions. Freedom of movement around hinge 1 provides a mechanism for lipid binding in almost any orientation relative to the G-domain. Whether Cj-DLP1 hinge 1 folds like BDLP1 remains to be determined. c Cartoon superposition of Cj-DLP1α and Mitofusin 1 partial structure26. Cj-DLP1AD has been removed for clarity. Neck and equivalent HD1 domains were aligned and show high similarity with helices running in phase. G-domains are offset by an 8° rotation around Gly436. Structural and conformational similarity between Cj-DLP1 and Mitofusin 1 suggests Cj-DLP1 is likely representative of full length Mitofusin 1
