Structural characterization of full-length NSF and 20S particles

Lei Fu Chang, Song Chen, Cui Cui Liu, Xijiang Pan, Jiansen Jiang, Xiao Chen Bai, Xin Xie, Hong Wei Wang, Sen Fang Sui

Research output: Contribution to journalArticle

38 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)268-275
Number of pages8
JournalNature Structural and Molecular Biology
Volume19
Issue number3
DOIs
StatePublished - Mar 1 2012

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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    Chang, L. F., Chen, S., Liu, C. C., Pan, X., Jiang, J., Bai, X. C., Xie, X., Wang, H. W., & Sui, S. F. (2012). Structural characterization of full-length NSF and 20S particles. Nature Structural and Molecular Biology, 19(3), 268-275. https://doi.org/10.1038/nsmb.2237