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TitleStructural characterization of full-length NSF and 20S particles.
Journal, issue, pagesNat Struct Mol Biol, Vol. 19, Issue 3, Page 268-275, Year 2012
Publish dateFeb 5, 2012
AuthorsLei-Fu Chang / Song Chen / Cui-Cui Liu / Xijiang Pan / Jiansen Jiang / Xiao-Chen Bai / Xin Xie / Hong-Wei Wang / Sen-Fang Sui /
PubMed AbstractThe 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 ...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.
External linksNat Struct Mol Biol / PubMed:22307055
MethodsEM (single particle)
Resolution9.2 - 10.0 Å
Structure data

EMDB-5370:
Cryo-EM structure of full-length NSF in the ADP-AlFx state
Method: EM (single particle) / Resolution: 9.2 Å

EMDB-5371:
Cryo-EM structure of full-length NSF in the ADP state
Method: EM (single particle) / Resolution: 10.0 Å

Source
  • Cricetulus griseus (Chinese hamster)

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