3J99

Structure of 20S supercomplex determined by single particle cryoelectron microscopy (State IIIb)


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 8.20 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Mechanistic insights into the recycling machine of the SNARE complex.

Zhao, M.Wu, S.Zhou, Q.Vivona, S.Cipriano, D.J.Cheng, Y.Brunger, A.T.

(2015) Nature 518: 61-67

  • DOI: https://doi.org/10.1038/nature14148
  • Primary Citation of Related Structures:  
    3J94, 3J95, 3J96, 3J97, 3J98, 3J99

  • PubMed Abstract: 

    Evolutionarily conserved SNARE (soluble N-ethylmaleimide sensitive factor attachment protein receptors) proteins form a complex that drives membrane fusion in eukaryotes. The ATPase NSF (N-ethylmaleimide sensitive factor), together with SNAPs (soluble NSF attachment protein), disassembles the SNARE complex into its protein components, making individual SNAREs available for subsequent rounds of fusion. Here we report structures of ATP- and ADP-bound NSF, and the NSF/SNAP/SNARE (20S) supercomplex determined by single-particle electron cryomicroscopy at near-atomic to sub-nanometre resolution without imposing symmetry. Large, potentially force-generating, conformational differences exist between ATP- and ADP-bound NSF. The 20S supercomplex exhibits broken symmetry, transitioning from six-fold symmetry of the NSF ATPase domains to pseudo four-fold symmetry of the SNARE complex. SNAPs interact with the SNARE complex with an opposite structural twist, suggesting an unwinding mechanism. The interfaces between NSF, SNAPs, and SNAREs exhibit characteristic electrostatic patterns, suggesting how one NSF/SNAP species can act on many different SNARE complexes.


  • Organizational Affiliation

    Department of Molecular and Cellular Physiology, Howard Hughes Medical Institute, Stanford University, Stanford, California 94305, USA.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Vesicle-fusing ATPase
A, B, C, D, E
A, B, C, D, E, F
747Cricetulus griseusMutation(s): 0 
Gene Names: NSF
EC: 3.6.4.6
UniProt
Find proteins for P18708 (Cricetulus griseus)
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UniProt GroupP18708
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Alpha-soluble NSF attachment proteinG [auth H],
H [auth I],
I [auth J],
J [auth G]
297Rattus norvegicusMutation(s): 0 
Gene Names: NapaSnapSnapa
UniProt
Find proteins for P54921 (Rattus norvegicus)
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UniProt GroupP54921
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Vesicle-associated membrane protein 263Rattus norvegicusMutation(s): 0 
Gene Names: Vamp2Syb2
UniProt
Find proteins for P63045 (Rattus norvegicus)
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UniProt GroupP63045
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  • Reference Sequence
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Syntaxin-1A67Rattus norvegicusMutation(s): 0 
Gene Names: Stx1aSap
UniProt
Find proteins for P32851 (Rattus norvegicus)
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UniProt GroupP32851
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
Synaptosomal-associated protein 25188Rattus norvegicusMutation(s): 0 
Gene Names: Snap25Snap
UniProt
Find proteins for P60881 (Rattus norvegicus)
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UniProt GroupP60881
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 8.20 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONRELION

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-01-28
    Type: Initial release
  • Version 1.1: 2015-02-11
    Changes: Database references
  • Version 1.2: 2018-07-18
    Changes: Data collection
  • Version 1.3: 2024-02-21
    Changes: Data collection, Database references, Refinement description