1XI5

Clathrin D6 coat with auxilin J-domain


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 12.0 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

Structure of an auxilin-bound clathrin coat and its implications for the mechanism of uncoating

Fotin, A.Cheng, Y.Grigorieff, N.Walz, T.Harrison, S.C.Kirchhausen, T.

(2004) Nature 432: 649-653

  • DOI: https://doi.org/10.1038/nature03078
  • Primary Citation of Related Structures:  
    1XI5

  • PubMed Abstract: 

    Clathrin-coated pits invaginate from specific membrane compartments and pinch off as coated vesicles. These vesicles then uncoat rapidly once released. The Hsc70 molecular chaperone effects the uncoating reaction, and is guided to appropriate locations on clathrin lattices by the J-domain-containing co-chaperone molecule auxilin. This raises the question of how a local event such as ATP hydrolysis by Hsc70 can catalyse a global disassembly. Here, we have used electron cryomicroscopy to determine 12-A-resolution structures of in-vitro-assembled clathrin coats in association with a carboxy-terminal fragment of auxilin that contains both the clathrin-binding region and the J domain. We have located the auxilin fragment by computing differences between these structures and those lacking auxilin (described in an accompanying paper). Auxilin binds within the clathrin lattice near contacts between an inward-projecting C-terminal helical tripod and the crossing of two 'ankle' segments; it also contacts the terminal domain of yet another clathrin 'leg'. It therefore recruits Hsc70 to the neighbourhood of a set of critical interactions. Auxilin binding produces a local change in heavy-chain contacts, creating a detectable global distortion of the clathrin coat. We propose a mechanism by which local destabilization of the lattice promotes general uncoating.


  • Organizational Affiliation

    Biophysics Graduate Program, Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Clathrin heavy chain
A, B, C, D, E
A, B, C, D, E, F, G, H, I
1,630Bos taurusMutation(s): 0 
UniProt
Find proteins for P49951 (Bos taurus)
Explore P49951 
Go to UniProtKB:  P49951
Entity Groups  
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UniProt GroupP49951
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Auxilin J-domain
J, K, L, M, N
J, K, L, M, N, O, P, Q, R
114Bos taurusMutation(s): 0 
UniProt
Find proteins for Q27974 (Bos taurus)
Explore Q27974 
Go to UniProtKB:  Q27974
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ27974
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 12.0 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONFREALIGN
RECONSTRUCTIONIMAGIC

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-11-02
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2019-10-09
    Changes: Data collection, Database references, Other
  • Version 1.4: 2019-12-18
    Changes: Data collection
  • Version 1.5: 2024-03-13
    Changes: Data collection, Database references, Derived calculations, Refinement description