5A1V

The structure of the COPI coat linkage I


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 21.0 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: TOMOGRAPHY 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Vesicular Transport. A Structure of the Copi Coat and the Role of Coat Proteins in Membrane Vesicle Assembly.

Dodonova, S.O.Diestelkoetter-Bachert, P.Von Appen, A.Hagen, W.J.H.Beck, R.Beck, M.Wieland, F.Briggs, J.A.G.

(2015) Science 349: 195

  • DOI: https://doi.org/10.1126/science.aab1121
  • Primary Citation of Related Structures:  
    5A1U, 5A1V, 5A1W, 5A1X, 5A1Y

  • PubMed Abstract: 

    Transport of material within cells is mediated by trafficking vesicles that bud from one cellular compartment and fuse with another. Formation of a trafficking vesicle is driven by membrane coats that localize cargo and polymerize into cages to bend the membrane. Although extensive structural information is available for components of these coats, the heterogeneity of trafficking vesicles has prevented an understanding of how complete membrane coats assemble on the membrane. We combined cryo-electron tomography, subtomogram averaging, and cross-linking mass spectrometry to derive a complete model of the assembled coat protein complex I (COPI) coat involved in traffic between the Golgi and the endoplasmic reticulum. The highly interconnected COPI coat structure contradicted the current "adaptor-and-cage" understanding of coated vesicle formation.


  • Organizational Affiliation

    Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Meyerhofstrasse 1, 69117 Heidelberg, Germany.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ADP-RIBOSYLATION FACTOR 1
A, B, I, J, R
A, B, I, J, R, S
181Saccharomyces cerevisiaeMutation(s): 0 
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
COATOMER SUBUNIT ALPHA
C, K, T
1,262Mus musculusMutation(s): 0 
UniProt
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
COATOMER SUBUNIT BETA
D, L, U
905Mus musculusMutation(s): 0 
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IMPC:  MGI:1354962
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
COATOMER SUBUNIT GAMMA-1
E, M, V
874Mus musculusMutation(s): 0 
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
COATOMER SUBUNIT ZETA-1
F, N, W
177Mus musculusMutation(s): 0 
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Entity ID: 6
MoleculeChains Sequence LengthOrganismDetailsImage
COATOMER SUBUNIT BETA'
G, O, X
968Mus musculusMutation(s): 0 
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Entity ID: 7
MoleculeChains Sequence LengthOrganismDetailsImage
COATOMER SUBUNIT DELTA
H, P, Y
511Mus musculusMutation(s): 0 
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IMPC:  MGI:2387591
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Entity ID: 8
MoleculeChains Sequence LengthOrganismDetailsImage
COATOMER SUBUNIT EPSILON
Q, Z
308Mus musculusMutation(s): 0 
UniProt
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Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 21.0 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: TOMOGRAPHY 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONAV3
RECONSTRUCTIONTOM Toolbox

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-07-08
    Type: Initial release
  • Version 1.1: 2015-07-22
    Changes: Database references, Derived calculations, Other
  • Version 1.2: 2017-08-30
    Changes: Data collection, Derived calculations, Refinement description