2X2E

Dynamin GTPase dimer, long axis form

Summary for 2X2E

• Entry DOI: 10.2210/pdb2x2e/pdb
• Related: 1DYN 2DYN 2X2F
• Descriptor: DYNAMIN-1, GUANOSINE-5'-DIPHOSPHATE, TETRAFLUOROALUMINATE ION, ... (6 entities in total)
• Functional Keywords: nitration, hydrolase, membrane fission, nucleotide-binding, endocytosis, motor protein
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 2
• Total formula weight: 80715.18

Authors

Chappie, J.S.,Acharya, S.,Leonard, M.,Schmid, S.L.,Dyda, F. (deposition date: 2010-01-12, release date: 2010-04-28, Last modification date: 2024-11-13)

Primary citation

Chappie, J.S.,Acharya, S.,Leonard, M.,Schmid, S.L.,Dyda, F.
G Domain Dimerization Controls Dynamin'S Assembly-Stimulated Gtpase Activity.
Nature, 465:435-, 2010

PubMed Abstract: 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.

PubMed: 20428113
DOI: 10.1038/NATURE09032

Experimental method

X-RAY DIFFRACTION (2 Å)