4BZK

The structure of the COPII coat assembled on membranes


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 40.0 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SUBTOMOGRAM AVERAGING 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

The Structure of the Copii Transport-Vesicle Coat Assembled on Membranes

Zanetti, G.Prinz, S.Daum, S.Meister, A.Schekman, R.Bacia, K.Briggs, J.A.G.

(2013) Elife 2: 00951

  • DOI: https://doi.org/10.7554/eLife.00951
  • Primary Citation of Related Structures:  
    4BZI, 4BZJ, 4BZK

  • PubMed Abstract: 

    Coat protein complex II (COPII) mediates formation of the membrane vesicles that export newly synthesised proteins from the endoplasmic reticulum. The inner COPII proteins bind to cargo and membrane, linking them to the outer COPII components that form a cage around the vesicle. Regulated flexibility in coat architecture is essential for transport of a variety of differently sized cargoes, but structural data on the assembled coat has not been available. We have used cryo-electron tomography and subtomogram averaging to determine the structure of the complete, membrane-assembled COPII coat. We describe a novel arrangement of the outer coat and find that the inner coat can assemble into regular lattices. The data reveal how coat subunits interact with one another and with the membrane, suggesting how coordinated assembly of inner and outer coats can mediate and regulate packaging of vesicles ranging from small spheres to large tubular carriers. DOI:http://dx.doi.org/10.7554/eLife.00951.001.


  • Organizational Affiliation

    Department of Molecular and Cell Biology , University of California, Berkeley , Berkeley , United States.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Protein transport protein SEC31
A, C
1,273Saccharomyces cerevisiaeMutation(s): 0 
Gene Names: SEC31WEB1YDL195WD1229
UniProt
Find proteins for P38968 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P38968 
Go to UniProtKB:  P38968
Entity Groups  
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UniProt GroupP38968
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Protein transport protein SEC13297Saccharomyces cerevisiaeMutation(s): 0 
Gene Names: SEC13ANU3YLR208WL8167.4
UniProt
Find proteins for Q04491 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore Q04491 
Go to UniProtKB:  Q04491
Entity Groups  
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UniProt GroupQ04491
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Protein transport protein SEC13D [auth F]297Saccharomyces cerevisiaeMutation(s): 0 
Gene Names: SEC13ANU3YLR208WL8167.4
UniProt
Find proteins for Q04491 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore Q04491 
Go to UniProtKB:  Q04491
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ04491
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 40.0 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SUBTOMOGRAM AVERAGING 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONAV3
RECONSTRUCTIONMATLAB
RECONSTRUCTIONTOM Toolbox

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-09-18
    Type: Initial release
  • Version 1.1: 2013-10-09
    Changes: Database references
  • Version 1.2: 2017-08-30
    Changes: Data collection, Experimental preparation, Refinement description
  • Version 1.3: 2019-09-11
    Changes: Data collection, Database references, Source and taxonomy, Structure summary