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Fig. 1. Dynamin self-assembles and tubulates lipids. (A) Scheme of dynamin protein showing the GTPase domain, the middle domain (MID), the pleckstrin-homology domain (PH), the GED domain, and the proline-rich domain (PRD). (B) Negative stain showing that dynamin protein self-assembles into rings in the presence of GTP
S; adapted from Hinshaw (Hinshaw, 2000), reprinted with permission. (C) The surface rendering depicts dynamin's ability to constrict around tubules in an ordered manner. The dynamin head domain is shown in green, the stalk is blue, the leg is gold, and the inner lipid leaflet is grey; adapted from Zhang and Hinshaw (Zhang and Hinshaw, 2001), reprinted with permission. Cryo-EM of 
PRD tubules before (D) and 5 seconds after (E) addition of GTP. The diagrams below each panel depict the constriction of the tubules in the presence of GTP. White arrows indicate undecorated lipid bulges and black arrowheads indicate transitions between constricted, decorated tubules and lipid bulges; adapted from Danino et al. (Danino et al., 2004), reprinted with permission. Bar, 100 nm. Negative stain of GDP-AlF (F) and GDP (G) dynamin on tubules depicting the change in pitch of dynamin rings after hydrolysis of GTP occurs; adapted from Stowell et al. (Stowell et al., 1999), reprinted with permission.
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