| First Author | Chappie JS | Year | 2010 |
| Journal | Nature | Volume | 465 |
| Issue | 7297 | Pages | 435-40 |
| PubMed ID | 20428113 | Mgi Jnum | J:341397 |
| Mgi Id | MGI:7539443 | Doi | 10.1038/nature09032 |
| Citation | Chappie JS, et al. (2010) G domain dimerization controls dynamin's assembly-stimulated GTPase activity. Nature 465(7297):435-40 |
| abstractText | Dynamin is an atypical GTPase that catalyses membrane fission during clathrin-mediated endocytosis. The mechanisms of dynamin's basal and assembly-stimulated GTP hydrolysis are unknown, though both are indirectly influenced by the GTPase effector domain (GED). Here we present the 2.0 A resolution crystal structure of a human dynamin 1-derived minimal GTPase-GED fusion protein, which was dimeric in the presence of the transition state mimic GDP.AlF(4)(-).The structure reveals dynamin's catalytic machinery and explains how assembly-stimulated GTP hydrolysis is achieved through G domain dimerization. A sodium ion present in the active site suggests that dynamin uses a cation to compensate for the developing negative charge in the transition state in the absence of an arginine finger. Structural comparison to the rat dynamin G domain reveals key conformational changes that promote G domain dimerization and stimulated hydrolysis. The structure of the GTPase-GED fusion protein dimer provides insight into the mechanisms underlying dynamin-catalysed membrane fission. |
