2XBO

Equine Rhinitis A Virus in Complex with its Sialic Acid Receptor


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 4.00 Å
  • R-Value Work: 0.247 
  • R-Value Observed: 0.247 

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This is version 2.0 of the entry. See complete history


Literature

The Crystal Structure of Equine Rhinitis a Virus in Complex with its Sialic Acid Receptor.

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

(2010) J Gen Virol 91: 1971

  • DOI: https://doi.org/10.1099/vir.0.020420-0
  • Primary Citation of Related Structures:  
    2XBO

  • PubMed Abstract: 

    Equine rhinitis A virus (ERAV) shares many features with foot-and-mouth disease virus (FMDV) and both are classified within the genus Aphthovirus of the family Picornaviridae. ERAV is used as a surrogate for FMDV research as it does not require high-level biosecurity. In contrast to FMDV, which uses integrins as cellular receptors, the receptor for ERAV has been reported to involve the sugar moiety sialic acid. This study confirmed the importance of sialic acid for cell entry by ERAV and reports the crystal structure of ERAV particles complexed with the receptor analogue 3'-sialyllactose. The receptor is attached to the rim of a capsid pit adjacent to the major immunogenic site and distinct from the sialic acid binding site used by a related picornavirus, the cardiovirus Theiler's murine encephalitis virus. The structure of the major antigenic determinant of the virus, previously identified from antibody escape mutations, is also described as the EF loop of VP1, which forms a hairpin stretching across the capsid surface close to the icosahedral fivefold axis, neighbouring the receptor-binding site, and spanning two protomeric units.


  • Organizational Affiliation

    Division of Structural Biology and Oxford Protein Production Facility, The Henry Wellcome Building for Genomic Medicine, Roosevelt Drive, Headington, Oxford OX3 7BN, UK.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
P1A [auth 1]248Equine 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
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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
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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
Oligosaccharides

Help

Entity ID: 5
MoleculeChains Length2D Diagram Glycosylation3D Interactions
N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-alpha-D-glucopyranoseE [auth A]3N/A
Glycosylation Resources
GlyTouCan:  G92323ZH
GlyCosmos:  G92323ZH
GlyGen:  G92323ZH
Biologically Interesting Molecules (External Reference) 1 Unique
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 4.00 Å
  • R-Value Work: 0.247 
  • R-Value Observed: 0.247 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 344.8α = 90
b = 531.4β = 90
c = 488.3γ = 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: 2010-09-22
    Type: Initial release
  • Version 2.0: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Atomic model, Data collection, Derived calculations, Other, Structure summary