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Title | Structural characterization of full-length NSF and 20S particles. |
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Journal, issue, pages | Nat Struct Mol Biol, Vol. 19, Issue 3, Page 268-275, Year 2012 |
Publish date | Feb 5, 2012 |
Authors | Lei-Fu Chang / Song Chen / Cui-Cui Liu / Xijiang Pan / Jiansen Jiang / Xiao-Chen Bai / Xin Xie / Hong-Wei Wang / Sen-Fang Sui / |
PubMed 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 ...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 links | Nat Struct Mol Biol / PubMed:22307055 |
Methods | EM (single particle) |
Resolution | 9.2 - 10.0 Å |
Structure data | EMDB-5370: EMDB-5371: |
Source |
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