1ES6

CRYSTAL STRUCTURE OF THE MATRIX PROTEIN OF EBOLA VIRUS


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.250 
  • R-Value Work: 0.220 
  • R-Value Observed: 0.223 

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This is version 1.4 of the entry. See complete history


Literature

Crystal structure of the matrix protein VP40 from Ebola virus.

Dessen, A.Volchkov, V.Dolnik, O.Klenk, H.D.Weissenhorn, W.

(2000) EMBO J 19: 4228-4236

  • DOI: https://doi.org/10.1093/emboj/19.16.4228
  • Primary Citation of Related Structures:  
    1ES6

  • PubMed Abstract: 

    Ebola virus maturation occurs at the plasma membrane of infected cells and involves the clustering of the viral matrix protein VP40 at the assembly site as well as its interaction with the lipid bilayer. Here we report the X-ray crystal structure of VP40 from Ebola virus at 2.0 A resolution. The crystal structure reveals that Ebola virus VP40 is topologically distinct from all other known viral matrix proteins, consisting of two domains with unique folds, connected by a flexible linker. The C-terminal domain, which is absolutely required for membrane binding, contains large hydrophobic patches that may be involved in the interaction with lipid bilayers. Likewise, a highly basic region is shared between the two domains. The crystal structure reveals how the molecule may be able to switch from a monomeric conformation to a hexameric form, as observed in vitro. Its implications for the assembly process are discussed.


  • Organizational Affiliation

    European Molecular Biology Laboratory Grenoble Outstation, 6 rue Jules Horowitz, 38000 Grenoble, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
MATRIX PROTEIN VP40296Ebola virus sp.Mutation(s): 1 
Membrane Entity: Yes 
UniProt
Find proteins for Q77DJ6 (Zaire ebolavirus (strain Kikwit-95))
Explore Q77DJ6 
Go to UniProtKB:  Q77DJ6
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ77DJ6
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.250 
  • R-Value Work: 0.220 
  • R-Value Observed: 0.223 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 64.637α = 90
b = 91.094β = 97.35
c = 49.226γ = 90
Software Package:
Software NamePurpose
SHARPphasing
CNSrefinement
DENZOdata reduction
SCALEPACKdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-08-30
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2021-11-03
    Changes: Database references
  • Version 1.4: 2024-02-07
    Changes: Data collection