Structural characterization of full-length NSF and 20S particles
Copyright policy )Structural characterization of full-length NSF and 20S particles
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.
- University of California, Los Angeles United States
- Tsinghua University China (People's Republic of)
Models, Molecular, Cryoelectron Microscopy, Protein Structure, Tertiary, Substrate Specificity, Adenosine Diphosphate, Adaptor Proteins, Vesicular Transport, Cricetulus, Structural Homology, Protein, Cricetinae, Animals, Protein Structure, Quaternary, SNARE Proteins, N-Ethylmaleimide-Sensitive Proteins, Protein Binding
Models, Molecular, Cryoelectron Microscopy, Protein Structure, Tertiary, Substrate Specificity, Adenosine Diphosphate, Adaptor Proteins, Vesicular Transport, Cricetulus, Structural Homology, Protein, Cricetinae, Animals, Protein Structure, Quaternary, SNARE Proteins, N-Ethylmaleimide-Sensitive Proteins, Protein Binding
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