4uud | pdb_00004uud

Human dynamin 1 K44A superconstricted polymer stabilized with GTP

spinqualitylabelsall models 4uud, resolution 12.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4uud is a 12 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 4uuk Activity: Dynamin GTPase, with EC number 3.6.5.5 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Dynamin is a 100 kDa GTPase that organizes into helical assemblies at the base of nascent clathrin-coated vesicles. Formation of these oligomers stimulates the intrinsic GTPase activity of dynamin, which is necessary for efficient membrane fission during endocytosis. Recent evidence suggests that the transition state of dynamin's GTP hydrolysis reaction serves as a key determinant of productive fission. Here, we present the structure of a transition-state-defective dynamin mutant K44A trapped in a prefission state at 12.5 A resolution. This structure constricts to 3.7 nm, reaching the theoretical limit required for spontaneous membrane fission. Computational docking indicates that the ground-state conformation of the dynamin polymer is sufficient to achieve this superconstricted prefission state and reveals how a two-start helical symmetry promotes the most efficient packing of dynamin tetramers around the membrane neck. These data suggest a model for the assembly and regulation of the minimal dynamin fission machine. A dynamin mutant defines a superconstricted prefission state.,Sundborger AC, Fang S, Heymann JA, Ray P, Chappie JS, Hinshaw JE Cell Rep. 2014 Aug 7;8(3):734-42. doi: 10.1016/j.celrep.2014.06.054. Epub 2014, Jul 31. PMID:25088425 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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