EMD-5371
Cryo-EM structure of full-length NSF in the ADP state
EMD-5371
Single-particle10.0 Å
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Map released: 01/02/2012
Last modified: 01/02/2012
Sample Organism:
Cricetulus griseus
Sample: N-ethylmaleimide-sensitive factor (NSF)
Deposition Authors: Chang LF, Chen S
,
Liu CC,
Pan X,
Jiang J,
Bai XC
,
Xie X,
Wang HW,
Sui SF
Sample: N-ethylmaleimide-sensitive factor (NSF)
Deposition Authors: Chang LF, Chen S
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Structural characterization of full-length NSF and 20S particles.
Chang LF,
Chen S
,
Liu CC,
Pan X,
Jiang J,
Bai XC
,
Xie X,
Wang HW,
Sui SF
(2012) Nat. Struct. Mol. Biol. , 19 , 268 - 275
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(2012) Nat. Struct. Mol. Biol. , 19 , 268 - 275
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.
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.