5BXZ

H17 Bat Influenza NS1 RNA Binding Domain


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.274 
  • R-Value Work: 0.173 
  • R-Value Observed: 0.184 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Novel Bat Influenza Virus NS1 Proteins Bind Double-Stranded RNA and Antagonize Host Innate Immunity.

Turkington, H.L.Juozapaitis, M.Kerry, P.S.Aydillo, T.Ayllon, J.Garcia-Sastre, A.Schwemmle, M.Hale, B.G.

(2015) J Virol 89: 10696-10701

  • DOI: https://doi.org/10.1128/JVI.01430-15
  • Primary Citation of Related Structures:  
    5BXZ, 5BY1

  • PubMed Abstract: 

    We demonstrate that novel bat HL17NL10 and HL18NL11 influenza virus NS1 proteins are effective interferon antagonists but do not block general host gene expression. Solving the RNA-binding domain structures revealed the canonical NS1 symmetrical homodimer, and RNA binding required conserved basic residues in this domain. Interferon antagonism was strictly dependent on RNA binding, and chimeric bat influenza viruses expressing NS1s defective in this activity were highly attenuated in interferon-competent cells but not in cells unable to establish antiviral immunity.


  • Organizational Affiliation

    Institute of Medical Virology, University of Zurich, Zurich, Switzerland.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Non-structural protein 1
A, B
84Influenza A virus (A/little yellow-shouldered bat/Guatemala/153/2009(H17N10))Mutation(s): 0 
Gene Names: NS1
UniProt
Find proteins for H6QM79 (Influenza A virus (strain A/little yellow-shouldered bat/Guatemala/153/2009(H17N10)))
Explore H6QM79 
Go to UniProtKB:  H6QM79
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupH6QM79
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.274 
  • R-Value Work: 0.173 
  • R-Value Observed: 0.184 
  • Space Group: P 41
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 46.675α = 90
b = 46.675β = 90
c = 60.23γ = 90
Software Package:
Software NamePurpose
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
PHENIXrefinement
PDB_EXTRACTdata extraction

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Medical Research Council (United Kingdom)United Kingdom--
Swiss National Science FoundationSwitzerland31003A_159993

Revision History  (Full details and data files)

  • Version 1.0: 2015-08-19
    Type: Initial release
  • Version 1.1: 2015-09-30
    Changes: Database references
  • Version 1.2: 2017-09-13
    Changes: Author supporting evidence
  • Version 1.3: 2024-05-08
    Changes: Data collection, Database references