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- Title
Structural characterization of full-length NSF and 20S particles.
- Authors
Chang, Lei-Fu; Chen, Song; Liu, Cui-Cui; Pan, Xijiang; Jiang, Jiansen; Bai, Xiao-Chen; Xie, Xin; Wang, Hong-Wei; Sui, Sen-Fang
- 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.
- Publication
Nature structural & molecular biology, 2012, Vol 19, Issue 3, p268
- ISSN
1545-9985
- Publication type
Journal Article
- DOI
10.1038/nsmb.2237