1TMF

THREE-DIMENSIONAL STRUCTURE OF THEILER MURINE ENCEPHALOMYELITIS VIRUS (BEAN STRAIN)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.50 Å

wwPDB Validation   3D Report Full Report


This is version 2.0 of the entry. See complete history


Literature

Three-dimensional structure of Theiler murine encephalomyelitis virus (BeAn strain).

Luo, M.He, C.Toth, K.S.Zhang, C.X.Lipton, H.L.

(1992) Proc Natl Acad Sci U S A 89: 2409-2413

  • DOI: https://doi.org/10.1073/pnas.89.6.2409
  • Primary Citation of Related Structures:  
    1TMF

  • PubMed Abstract: 

    Depending on the strain, Theiler murine encephalomyelitis virus (TMEV) may cause acute encephalitis or chronic demyelinating disease, which is associated with viral persistence in mice. Persistent central nervous system infection and demyelination by the less-virulent TMEV has provided a useful animal model for the human demyelinating disease multiple sclerosis. The less-virulent BeAn strain of TMEV was crystallized and its atomic structure was determined by x-ray crystallography. The alpha-carbon coordinates of the closely related Mengo virus were used to calculate the initial phases to 3.5 A resolution and the interpretable electron density map was produced by 10 cycles of 30-fold noncrystallographic molecular replacement averaging. The structure revealed a high degree of overall structural similarity to Mengo virus as well as substantial differences in the surface loops. These structural changes might be correlated with TMEV host-specific recognition, pH-related stability, and neurovirulence.


  • Organizational Affiliation

    Department of Microbiology, University of Alabama, Birmingham 35294.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
THEILER'S MURINE ENCEPHALOMYELITIS VIRUS (SUBUNIT VP1)A [auth 1]276Theiler's encephalomyelitis virusMutation(s): 0 
UniProt
Find proteins for P08544 (Theiler's murine encephalomyelitis virus (strain BeAn 8386))
Explore P08544 
Go to UniProtKB:  P08544
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP08544
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
THEILER'S MURINE ENCEPHALOMYELITIS VIRUS (SUBUNIT VP2)B [auth 2]267Theiler's encephalomyelitis virusMutation(s): 0 
UniProt
Find proteins for P08544 (Theiler's murine encephalomyelitis virus (strain BeAn 8386))
Explore P08544 
Go to UniProtKB:  P08544
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP08544
Sequence Annotations
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
THEILER'S MURINE ENCEPHALOMYELITIS VIRUS (SUBUNIT VP3)C [auth 3]232Theiler's encephalomyelitis virusMutation(s): 0 
UniProt
Find proteins for P08544 (Theiler's murine encephalomyelitis virus (strain BeAn 8386))
Explore P08544 
Go to UniProtKB:  P08544
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP08544
Sequence Annotations
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  • Reference Sequence
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
THEILER'S MURINE ENCEPHALOMYELITIS VIRUS (SUBUNIT VP4)D [auth 4]45Theiler's encephalomyelitis virusMutation(s): 0 
UniProt
Find proteins for P13899 (Theiler's murine encephalomyelitis virus (strain DA))
Explore P13899 
Go to UniProtKB:  P13899
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP13899
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.50 Å
  • Space Group: P 43 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 331.86α = 90
b = 331.86β = 90
c = 796.26γ = 90

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1993-10-31
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 2.0: 2023-04-19
    Type: Remediation
    Changes: Advisory, Atomic model, Data collection, Database references, Derived calculations, Other, Refinement description