3M8L

Crystal Structure Analysis of the Feline Calicivirus Capsid Protein


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.40 Å
  • R-Value Free: 0.370 
  • R-Value Work: 0.390 
  • R-Value Observed: 0.390 

wwPDB Validation   3D Report Full Report


This is version 2.1 of the entry. See complete history


Literature

Conformational changes in the capsid of a calicivirus upon interaction with its functional receptor

Ossiboff, R.J.Zhou, Y.Lightfoot, P.J.Prasad, B.V.Parker, J.S.

(2010) J Virol 84: 5550-5564

  • DOI: https://doi.org/10.1128/JVI.02371-09
  • Primary Citation of Related Structures:  
    3M8L

  • PubMed Abstract: 

    Nonenveloped viral capsids are metastable structures that undergo conformational changes during virus entry that lead to interactions of the capsid or capsid fragments with the cell membrane. For members of the Caliciviridae, neither the nature of these structural changes in the capsid nor the factor(s) responsible for inducing these changes is known. Feline junctional adhesion molecule A (fJAM-A) mediates the attachment and infectious viral entry of feline calicivirus (FCV). Here, we show that the infectivity of some FCV isolates is neutralized following incubation with the soluble receptor at 37 degrees C. We used this property to select mutants resistant to preincubation with the soluble receptor. We isolated and sequenced 24 soluble receptor-resistant (srr) mutants and characterized the growth properties and receptor-binding activities of eight mutants. The location of the mutations within the capsid structure of FCV was mapped using a new 3.6-A structure of native FCV. The srr mutations mapped to the surface of the P2 domain were buried at the protruding domain dimer interface or were present in inaccessible regions of the capsid protein. Coupled with data showing that both the parental FCV and the srr mutants underwent increases in hydrophobicity upon incubation with the soluble receptor at 37 degrees C, these findings indicate that FCV likely undergoes conformational change upon interaction with its receptor. Changes in FCV capsid conformation following its interaction with fJAM-A may be important for subsequent interactions of the capsid with cellular membranes, membrane penetration, and genome delivery.


  • Organizational Affiliation

    Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Hungerford Hill Road, Ithaca, NY 14853, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Capsid protein
A, B, C
534Feline calicivirusMutation(s): 0 
UniProt
Find proteins for A2T4Q0 (Feline calicivirus)
Explore A2T4Q0 
Go to UniProtKB:  A2T4Q0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA2T4Q0
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.40 Å
  • R-Value Free: 0.370 
  • R-Value Work: 0.390 
  • R-Value Observed: 0.390 
  • Space Group: I 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 427.08α = 90
b = 450.726β = 90
c = 467.586γ = 90
Software Package:
Software NamePurpose
HKL-3000data collection
RAVEmodel building
CNSrefinement
d*TREKdata reduction
d*TREKdata scaling
RAVEphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-06-30
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 2.0: 2017-06-28
    Changes: Advisory, Atomic model, Database references, Derived calculations, Other, Polymer sequence, Source and taxonomy, Structure summary
  • Version 2.1: 2023-09-06
    Changes: Data collection, Database references, Derived calculations, Refinement description