2WJ8

Respiratory Syncitial Virus RiboNucleoProtein


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.29 Å
  • R-Value Free: 0.226 
  • R-Value Work: 0.205 
  • R-Value Observed: 0.206 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Crystal Structure of a Nucleocapsid-Like Nucleoprotein-RNA Complex of Respiratory Syncytial Virus

Tawar, R.G.Duquerroy, S.Vonrhein, C.Varela, P.F.Damier-Piolle, L.Castagne, N.Maclellan, K.Bedouelle, H.Bricogne, G.Bhella, D.Eleouet, J.Rey, F.A.

(2009) Science 326: 1279

  • DOI: https://doi.org/10.1126/science.1177634
  • Primary Citation of Related Structures:  
    2WJ8

  • PubMed Abstract: 

    The respiratory syncytial virus (RSV) is an important human pathogen, yet neither a vaccine nor effective therapies are available to treat infection. To help elucidate the replication mechanism of this RNA virus, we determined the three-dimensional (3D) crystal structure at 3.3 A resolution of a decameric, annular ribonucleoprotein complex of the RSV nucleoprotein (N) bound to RNA. This complex mimics one turn of the viral helical nucleocapsid complex, which serves as template for viral RNA synthesis. The RNA wraps around the protein ring, with seven nucleotides contacting each N subunit, alternating rows of four and three stacked bases that are exposed and buried within a protein groove, respectively. Combined with electron microscopy data, this structure provides a detailed model for the RSV nucleocapsid, in which the bases are accessible for readout by the viral polymerase. Furthermore, the nucleoprotein structure highlights possible key sites for drug targeting.


  • Organizational Affiliation

    Institut Pasteur, Unité de Virologie Structurale, Département de Virologie and CNRS Unité de Recherche Associée (URA) 3015, 25 Rue du Dr Roux, 75724 Paris Cedex 15, France.


Macromolecules

Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
NUCLEOPROTEIN
A, B, C, D, E
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T
391Human respiratory syncytial virus A strain LongMutation(s): 0 
UniProt
Find proteins for P03418 (Human respiratory syncytial virus A (strain A2))
Explore P03418 
Go to UniProtKB:  P03418
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03418
Sequence Annotations
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  • Reference Sequence

Find similar nucleic acids by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains LengthOrganismImage
RNA (5'-R(*CP*CP*CP*CP*CP*C)-3')7Escherichia coli BL21(DE3)
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
BO4
Query on BO4

Download Ideal Coordinates CCD File 
OA [auth A]
PA [auth B]
QA [auth C]
RA [auth D]
SA [auth H]
OA [auth A],
PA [auth B],
QA [auth C],
RA [auth D],
SA [auth H],
TA [auth I],
UA [auth K],
VA [auth L],
WA [auth M],
XA [auth N],
YA [auth O],
ZA [auth T]
BORATE ION
B H4 O4
KCFLOKKYWBPKFN-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.29 Å
  • R-Value Free: 0.226 
  • R-Value Work: 0.205 
  • R-Value Observed: 0.206 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 218.2α = 90
b = 220.99β = 93.09
c = 218.1γ = 90
Software Package:
Software NamePurpose
XDSdata reduction
SCALAdata scaling
AMoREphasing
MOLREPphasing
BUSTER-TNTrefinement

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2009-12-08
    Type: Initial release
  • Version 1.1: 2013-04-17
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description, Version format compliance
  • Version 1.2: 2018-11-21
    Changes: Data collection, Derived calculations
  • Version 1.3: 2019-10-30
    Changes: Advisory, Data collection, Derived calculations, Other
  • Version 1.4: 2019-11-13
    Changes: Data collection, Database references