1QQP

FOOT-AND-MOUTH DISEASE VIRUS/ OLIGOSACCHARIDE RECEPTOR COMPLEX.


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Work: 0.161 
  • R-Value Observed: 0.161 

wwPDB Validation   3D Report Full Report


This is version 2.1 of the entry. See complete history


Literature

The structure and function of a foot-and-mouth disease virus-oligosaccharide receptor complex.

Fry, E.E.Lea, S.M.Jackson, T.Newman, J.W.Ellard, F.M.Blakemore, W.E.Abu-Ghazaleh, R.Samuel, A.King, A.M.Stuart, D.I.

(1999) EMBO J 18: 543-554

  • DOI: https://doi.org/10.1093/emboj/18.3.543
  • Primary Citation of Related Structures:  
    1QQP

  • PubMed Abstract: 

    Heparan sulfate has an important role in cell entry by foot-and-mouth disease virus (FMDV). We find that subtype O1 FMDV binds this glycosaminoglycan with a high affinity by immobilizing a specific highly abundant motif of sulfated sugars. The binding site is a shallow depression on the virion surface, located at the junction of the three major capsid proteins, VP1, VP2 and VP3. Two pre-formed sulfate-binding sites control receptor specificity. Residue 56 of VP3, an arginine in this virus, is critical to this recognition, forming a key component of both sites. This residue is a histidine in field isolates of the virus, switching to an arginine in adaptation to tissue culture, forming the high affinity heparan sulfate-binding site. We postulate that this site is a conserved feature of FMDVs, such that in the infected animal there is a biological advantage to low affinity, or more selective, interactions with glycosaminoglycan receptors.


  • Organizational Affiliation

    The Laboratory of Molecular Biophysics, Rex Richards Building, South Parks Road, Oxford OX1 3QU, UK.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (GENOME POLYPROTEIN)A [auth 1]213Foot-and-mouth disease virusMutation(s): 0 
UniProt
Find proteins for P03305 (Foot-and-mouth disease virus (isolate Bovine/Germany/O1Kaufbeuren/1966 serotype O))
Explore P03305 
Go to UniProtKB:  P03305
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03305
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (GENOME POLYPROTEIN)B [auth 2]218Foot-and-mouth disease virusMutation(s): 0 
UniProt
Find proteins for P03305 (Foot-and-mouth disease virus (isolate Bovine/Germany/O1Kaufbeuren/1966 serotype O))
Explore P03305 
Go to UniProtKB:  P03305
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03305
Sequence Annotations
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (GENOME POLYPROTEIN)C [auth 3]220Foot-and-mouth disease virusMutation(s): 0 
UniProt
Find proteins for P03305 (Foot-and-mouth disease virus (isolate Bovine/Germany/O1Kaufbeuren/1966 serotype O))
Explore P03305 
Go to UniProtKB:  P03305
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03305
Sequence Annotations
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  • Reference Sequence
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (GENOME POLYPROTEIN)D [auth 4]85Foot-and-mouth disease virusMutation(s): 0 
UniProt
Find proteins for P03305 (Foot-and-mouth disease virus (isolate Bovine/Germany/O1Kaufbeuren/1966 serotype O))
Explore P03305 
Go to UniProtKB:  P03305
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03305
Sequence Annotations
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  • Reference Sequence
Oligosaccharides

Help

Entity ID: 5
MoleculeChains Length2D Diagram Glycosylation3D Interactions
2-O-sulfo-alpha-L-gulopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-gulopyranuronic acidE [auth A]5N/A
Glycosylation Resources
GlyTouCan:  G80049LO
GlyCosmos:  G80049LO
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Work: 0.161 
  • R-Value Observed: 0.161 
  • Space Group: I 2 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 345α = 90
b = 345β = 90
c = 345γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
X-PLORrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1999-06-18
    Type: Initial release
  • Version 1.1: 2008-04-26
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Non-polymer description, Version format compliance
  • Version 2.0: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Advisory, Atomic model, Data collection, Database references, Derived calculations, Structure summary
  • Version 2.1: 2023-08-16
    Changes: Data collection, Database references, Derived calculations, Refinement description, Structure summary