4UUK: Human Dynamin 1 K44a Superconstricted Polymer Stabilized With Gtp Strand 2

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.
PDB ID: 4UUKDownload
MMDB ID: 122788
PDB Deposition Date: 2014/7/29
Updated in MMDB: 2017/09
Experimental Method:
electron microscopy
Resolution: 12.5  Å
Source Organism:
Similar Structures:
Biological Unit for 4UUK: dodecameric; determined by software (PISA)
Molecular Components in 4UUK
Label Count Molecule
Proteins (12 molecules)
Dynamin-1(Gene symbol: DNM1)
Molecule annotation
Dynamin-1(Gene symbol: DNM1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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