EMD-5371

Single-particle
10.0 Å
EMD-5371 Deposition: 15/12/2011
Map released: 01/02/2012
Last modified: 01/02/2012
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-5371

Cryo-EM structure of full-length NSF in the ADP state

EMD-5371

Single-particle
10.0 Å
EMD-5371 Deposition: 15/12/2011
Map released: 01/02/2012
Last modified: 01/02/2012
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Cricetulus griseus
Sample: N-ethylmaleimide-sensitive factor (NSF)

Deposition Authors: Chang LF, Chen S , Liu CC, Pan X, Jiang J, Bai XC , Xie X, Wang HW, Sui SF
Structural characterization of full-length NSF and 20S particles.
Chang LF, Chen S , Liu CC, Pan X, Jiang J, Bai XC , Xie X, Wang HW, Sui SF
(2012) Nat. Struct. Mol. Biol. , 19 , 268 - 275
Abstract:
The 20S particle, which is composed of the N-ethylmaleimide-sensitive factor (NSF), soluble NSF attachment proteins (SNAPs) and the SNAP receptor (SNARE) complex, has an essential role in intracellular vesicle fusion events. Using single-particle cryo-EM and negative stain EM, we reconstructed four related three-dimensional structures: Chinese hamster NSF hexamer in the ATPγS, ADP-AlFx and ADP states, and the 20S particle. These structures reveal a parallel arrangement between the D1 and D2 domains of the hexameric NSF and characterize the nucleotide-dependent conformational changes in NSF. The structure of the 20S particle shows that it holds the SNARE complex at two interaction interfaces around the C terminus and N-terminal half of the SNARE complex, respectively. These findings provide insight into the molecular mechanism underlying disassembly of the SNARE complex by NSF.