2x2f | pdb_00002x2f

DYNAMIN 1 GTPASE DIMER, SHORT AXIS FORM

spinqualitylabelsall models 2x2f, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2x2f is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. Ligands: ALF, GDP, MG, NA NonStd Res: MSE Related: 2dyn, 2x2e, 1dyn Activity: Glucokinase, with EC number 2.7.1.2 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. G domain dimerization controls dynamin's assembly-stimulated GTPase activity.,Chappie JS, Acharya S, Leonard M, Schmid SL, Dyda F Nature. 2010 May 27;465(7297):435-40. Epub 2010 Apr 28. PMID:20428113 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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