2WFF

Equine Rhinitis A Virus


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 4.00 Å
  • R-Value Work: 0.462 
  • R-Value Observed: 0.462 

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This is version 1.2 of the entry. See complete history


Literature

Equine Rhinitis a Virus and its Low Ph Empty Particle: Clues Towards an Aphthovirus Entry Mechanism?

Tuthill, T.J.Harlos, K.Walter, T.S.Knowles, N.J.Groppelli, E.Rowlands, D.J.Stuart, D.I.Fry, E.E.

(2009) PLoS Pathog 5: 620

  • DOI: https://doi.org/10.1371/journal.ppat.1000620
  • Primary Citation of Related Structures:  
    2WFF, 2WS9

  • PubMed Abstract: 

    Equine rhinitis A virus (ERAV) is closely related to foot-and-mouth disease virus (FMDV), belonging to the genus Aphthovirus of the Picornaviridae. How picornaviruses introduce their RNA genome into the cytoplasm of the host cell to initiate replication is unclear since they have no lipid envelope to facilitate fusion with cellular membranes. It has been thought that the dissociation of the FMDV particle into pentameric subunits at acidic pH is the mechanism for genome release during cell entry, but this raises the problem of how transfer across the endosome membrane of the genome might be facilitated. In contrast, most other picornaviruses form 'altered' particle intermediates (not reported for aphthoviruses) thought to induce membrane pores through which the genome can be transferred. Here we show that ERAV, like FMDV, dissociates into pentamers at mildly acidic pH but demonstrate that dissociation is preceded by the transient formation of empty 80S particles which have released their genome and may represent novel biologically relevant intermediates in the aphthovirus cell entry process. The crystal structures of the native ERAV virus and a low pH form have been determined via highly efficient crystallization and data collection strategies, required due to low virus yields. ERAV is closely similar to FMDV for VP2, VP3 and part of VP4 but VP1 diverges, to give a particle with a pitted surface, as seen in cardioviruses. The low pH particle has internal structure consistent with it representing a pre-dissociation cell entry intermediate. These results suggest a unified mechanism of picornavirus cell entry.


  • Organizational Affiliation

    Institute of Molecular and Cellular Biology and Astbury Centre for Structural Molecular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, United Kingdom.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
P1A [auth 1]246Equine rhinitis A virusMutation(s): 0 
UniProt
Find proteins for B9VV85 (Equine rhinitis A virus)
Explore B9VV85 
Go to UniProtKB:  B9VV85
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupB9VV85
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
P1B [auth 2]230Equine rhinitis A virusMutation(s): 0 
UniProt
Find proteins for B9VV85 (Equine rhinitis A virus)
Explore B9VV85 
Go to UniProtKB:  B9VV85
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupB9VV85
Sequence Annotations
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
P1C [auth 3]226Equine rhinitis A virusMutation(s): 0 
UniProt
Find proteins for B9VV85 (Equine rhinitis A virus)
Explore B9VV85 
Go to UniProtKB:  B9VV85
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupB9VV85
Sequence Annotations
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  • Reference Sequence
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
P1D [auth 4]80Equine rhinitis A virusMutation(s): 0 
UniProt
Find proteins for B9VV85 (Equine rhinitis A virus)
Explore B9VV85 
Go to UniProtKB:  B9VV85
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupB9VV85
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 4.00 Å
  • R-Value Work: 0.462 
  • R-Value Observed: 0.462 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 314α = 90
b = 497.8β = 92.35
c = 556.5γ = 90
Software Package:
Software NamePurpose
X-PLORrefinement
DENZOdata reduction
SCALEPACKdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-05-05
    Type: Initial release
  • Version 1.1: 2011-12-07
    Changes: Other, Version format compliance
  • Version 1.2: 2023-12-13
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description