6SCT

Cryo-EM structure of the consensus triskelion hub of the clathrin coat complex


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.69 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Cryo-EM of multiple cage architectures reveals a universal mode of clathrin self-assembly.

Morris, K.L.Jones, J.R.Halebian, M.Wu, S.Baker, M.Armache, J.P.Avila Ibarra, A.Sessions, R.B.Cameron, A.D.Cheng, Y.Smith, C.J.

(2019) Nat Struct Mol Biol 26: 890-898

  • DOI: https://doi.org/10.1038/s41594-019-0292-0
  • Primary Citation of Related Structures:  
    6SCT

  • PubMed Abstract: 

    Clathrin forms diverse lattice and cage structures that change size and shape rapidly in response to the needs of eukaryotic cells during clathrin-mediated endocytosis and intracellular trafficking. We present the cryo-EM structure and molecular model of assembled porcine clathrin, providing insights into interactions that stabilize key elements of the clathrin lattice, namely, between adjacent heavy chains, at the light chain-heavy chain interface and within the trimerization domain. Furthermore, we report cryo-EM maps for five different clathrin cage architectures. Fitting structural models to three of these maps shows that their assembly requires only a limited range of triskelion leg conformations, yet inherent flexibility is required to maintain contacts. Analysis of the protein-protein interfaces shows remarkable conservation of contact sites despite architectural variation. These data reveal a universal mode of clathrin assembly that allows variable cage architecture and adaptation of coated vesicle size and shape during clathrin-mediated vesicular trafficking or endocytosis.


  • Organizational Affiliation

    School of Life Sciences, University of Warwick, Coventry, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Clathrin heavy chain1,675Sus scrofaMutation(s): 0 
Gene Names: CLTC
UniProt
Find proteins for C0MHR2 (Sus scrofa)
Explore C0MHR2 
Go to UniProtKB:  C0MHR2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupC0MHR2
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Clathrin light chain229Sus scrofaMutation(s): 0 
Gene Names: CLTB
UniProt
Find proteins for F1S398 (Sus scrofa)
Explore F1S398 
Go to UniProtKB:  F1S398
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupF1S398
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.69 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONRELION2.1

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Biotechnology and Biological Sciences Research CouncilUnited KingdomBB/K003461/1
Biotechnology and Biological Sciences Research CouncilUnited KingdomBB/N008391/1
Biotechnology and Biological Sciences Research CouncilUnited KingdomBB/L018888/1

Revision History  (Full details and data files)

  • Version 1.0: 2019-10-02
    Type: Initial release
  • Version 1.1: 2019-10-16
    Changes: Data collection, Database references
  • Version 1.2: 2019-11-06
    Changes: Data collection, Refinement description
  • Version 1.3: 2019-12-18
    Changes: Advisory
  • Version 1.4: 2024-05-15
    Changes: Data collection, Database references