Fig. 3
From: Structural basis for membrane tethering by a bacterial dynamin-like pair
Structural analysis of Cj-DLP2 bound to GDP·AlF4¯. a Cartoon comparison of Cj-DLP2 monomer with the ETEC DLP LeoA. Blue represents N-terminus through to the red C-terminus. Cj-DLP2 and LeoA have similar neck and trunk architecture with RMSD = 7.0 Å when superimposed (right panel). No distinct hinge 1 region is observed at the neck-trunk interface. The Cj-DLP2 GTPase domain is in a hinge 2 closed position and requires a complex two plane twist to generate the LeoA GTPase domain conformation (open position). The lipid binding domain includes residues 530FVLF534 and is disordered in the model. b SEC-MALS shows that removal of the Cj-DLP2 trunk tip (amino acids 348–401 and 509–542 coloured in red) abolishes Cj-DLP2 back-to-back cis dimerisation within Cj-DLP1/2tetramer, and results in Cj-DLP1/2 heterodimer instead. c Focus on the Cj-DLP2 back-to-back cis dimer showing all structural domains including the GTPase, neck and trunk contribute to the 5969 Å2 dimerisation interface. BDLP1 forms a similar back-to-back dimer when self-assembled as derived from the EM fitted model18
