4LDD

Crystal Structure of Ebola virus VP40 Hexamer


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.50 Å
  • R-Value Free: 0.323 
  • R-Value Work: 0.306 
  • R-Value Observed: 0.307 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structural Rearrangement of Ebola Virus VP40 Begets Multiple Functions in the Virus Life Cycle.

Bornholdt, Z.A.Noda, T.Abelson, D.M.Halfmann, P.Wood, M.R.Kawaoka, Y.Saphire, E.O.

(2013) Cell 154: 763-774

  • DOI: https://doi.org/10.1016/j.cell.2013.07.015
  • Primary Citation of Related Structures:  
    4LD8, 4LDB, 4LDD, 4LDI, 4LDM

  • PubMed Abstract: 

    Proteins, particularly viral proteins, can be multifunctional, but the mechanisms behind multifunctionality are not fully understood. Here, we illustrate through multiple crystal structures, biochemistry, and cellular microscopy that VP40 rearranges into different structures, each with a distinct function required for the ebolavirus life cycle. A butterfly-shaped VP40 dimer traffics to the cellular membrane. Once there, electrostatic interactions trigger rearrangement of the polypeptide into a linear hexamer. These hexamers construct a multilayered, filamentous matrix structure that is critical for budding and resembles tomograms of authentic virions. A third structure of VP40, formed by a different rearrangement, is not involved in virus assembly but instead uniquely binds RNA to regulate viral transcription inside infected cells. These results provide a functional model for ebolavirus matrix assembly and the other roles of VP40 in the virus life cycle and demonstrate how a single wild-type, unmodified polypeptide can assemble into different structures for different functions.


  • Organizational Affiliation

    Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, CA 92037, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Matrix protein VP40A [auth B],
B [auth C],
C [auth A]
297Zaire ebolavirusMutation(s): 0 
Gene Names: VP40
UniProt
Find proteins for Q05128 (Zaire ebolavirus (strain Mayinga-76))
Explore Q05128 
Go to UniProtKB:  Q05128
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ05128
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.50 Å
  • R-Value Free: 0.323 
  • R-Value Work: 0.306 
  • R-Value Observed: 0.307 
  • Space Group: P 4 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 134.479α = 90
b = 134.479β = 90
c = 136.087γ = 90
Software Package:
Software NamePurpose
HKL-2000data collection
PHASERphasing
PHENIXrefinement
d*TREKdata reduction
d*TREKdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-08-21
    Type: Initial release
  • Version 1.1: 2013-09-04
    Changes: Database references
  • Version 1.2: 2014-09-17
    Changes: Derived calculations
  • Version 1.3: 2024-02-28
    Changes: Data collection, Database references