3CJI

Structure of Seneca Valley Virus-001


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.260 
  • R-Value Work: 0.258 
  • R-Value Observed: 0.258 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structure of Seneca Valley Virus-001: an oncolytic picornavirus representing a new genus

Venkataraman, S.Reddy, S.P.Loo, J.Idamakanti, N.Hallenbeck, P.L.Reddy, V.S.

(2008) Structure 16: 1555-1561

  • DOI: https://doi.org/10.1016/j.str.2008.07.013
  • Primary Citation of Related Structures:  
    3CJI

  • PubMed Abstract: 

    The crystal structure of Seneca Valley Virus-001 (SVV-001), the representative member of a new genus, Senecavirus, is reported at 2.3A resolution. SVV-001 is the first naturally occurring nonpathogenic picornavirus shown to mediate selective cytotoxicity towards tumor cells with neuroendocrine cancer features. The nonsegmented (+) ssRNA genome of SVV-001 shares closest sequence similarity with the genomes of the members of Cardiovirus. The overall tertiary structure of VP1-VP4 subunits is conserved with the exception of loops, especially those of VP1 that show large deviations relative to the members of the cardioviruses. The surface loops of VP1 and VP2 are predicted to mediate cell tropism of SVV-001. In addition, the organization of the packaged nucleic acid density indicates that certain regions of VP2 and VP4 interact closely with the packaged nucleic acid.


  • Organizational Affiliation

    Department of Molecular Biology, TPC-6, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Polyprotein263Senecavirus AMutation(s): 0 
UniProt
Find proteins for Q155Z9 (Seneca Valley virus (isolate -/United States/SSV-001/2002))
Explore Q155Z9 
Go to UniProtKB:  Q155Z9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ155Z9
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Polyprotein239Senecavirus AMutation(s): 0 
UniProt
Find proteins for Q155Z9 (Seneca Valley virus (isolate -/United States/SSV-001/2002))
Explore Q155Z9 
Go to UniProtKB:  Q155Z9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ155Z9
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Polyprotein284Senecavirus AMutation(s): 0 
UniProt
Find proteins for Q155Z9 (Seneca Valley virus (isolate -/United States/SSV-001/2002))
Explore Q155Z9 
Go to UniProtKB:  Q155Z9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ155Z9
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Polyprotein71Senecavirus AMutation(s): 0 
UniProt
Find proteins for Q155Z9 (Seneca Valley virus (isolate -/United States/SSV-001/2002))
Explore Q155Z9 
Go to UniProtKB:  Q155Z9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ155Z9
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
CA
Query on CA

Download Ideal Coordinates CCD File 
E [auth B]CALCIUM ION
Ca
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.260 
  • R-Value Work: 0.258 
  • R-Value Observed: 0.258 
  • Space Group: H 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 311.51α = 90
b = 311.51β = 90
c = 1526.401γ = 120
Software Package:
Software NamePurpose
CNSrefinement
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-12-16
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2023-08-30
    Changes: Data collection, Database references, Derived calculations, Refinement description