2XGK

Virus like particle of L172W mutant of Minute Virus of Mice - the immunosuppressive strain


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 4.20 Å
  • R-Value Work: 0.303 
  • R-Value Observed: 0.303 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structure of a Packaging-Defective Mutant of Minute Virus of Mice Indicates that the Genome is Packaged Via a Pore at a 5-Fold Axis.

Plevka, P.Hafenstein, S.Li, L.D'Abrgamo, A.Cotmore, S.F.Rossmann, M.G.Tattersall, P.

(2011) J Virol 85: 4822

  • DOI: https://doi.org/10.1128/JVI.02598-10
  • Primary Citation of Related Structures:  
    2XGK

  • PubMed Abstract: 

    The parvovirus minute virus of mice (MVM) packages a single copy of its linear single-stranded DNA genome into preformed capsids, in a process that is probably driven by a virus-encoded helicase. Parvoviruses have a roughly cylindrically shaped pore that surrounds each of the 12 5-fold vertices. The pore, which penetrates the virion shell, is created by the juxtaposition of 10 antiparallel β-strands, two from each of the 5-fold-related capsid proteins. There is a bottleneck in the channel formed by the symmetry-related side chains of the leucines at position 172. We report here the X-ray crystal structure of the particles produced by a leucine-to-tryptophan mutation at position 172 and the analysis of its biochemical properties. The mutant capsid had its 5-fold channel blocked, and the particles were unable to package DNA, strongly suggesting that the 5-fold pore is the packaging portal for genome entry.


  • Organizational Affiliation

    Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
COAT PROTEIN VP2587Murine minute virus (STRAIN MVMI)Mutation(s): 1 
UniProt
Find proteins for P07302 (Murine minute virus (strain MVMi))
Explore P07302 
Go to UniProtKB:  P07302
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP07302
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 4.20 Å
  • R-Value Work: 0.303 
  • R-Value Observed: 0.303 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 442.9α = 90
b = 411.1β = 95.88
c = 301.8γ = 90
Software Package:
Software NamePurpose
HKL-2000data reduction
HKL-2000data scaling
GLRFphasing
CNSphasing
CNSrefinement

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-04-20
    Type: Initial release
  • Version 1.1: 2011-11-16
    Changes: Atomic model, Database references, Derived calculations, Other, Structure summary
  • Version 1.2: 2019-01-30
    Changes: Data collection, Experimental preparation, Other
  • Version 1.3: 2023-12-20
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description