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PDBsum entry 2wj8

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protein dna_rna ligands Protein-protein interface(s) links
RNA binding protein/RNA PDB id
2wj8
Jmol
Contents
Protein chains
(+ 14 more) 374 a.a. *
DNA/RNA
Ligands
BO4 ×12
Waters ×685
* Residue conservation analysis
PDB id:
2wj8
Name: RNA binding protein/RNA
Title: Respiratory syncitial virus ribonucleoprotein
Structure: Nucleoprotein. Chain: a, b, c, d, e, f, g, h, i, j, k, l, m, n, o, p, q, r, s, t. Synonym: protein n, nucleocapsid protein. Engineered: yes. RNA (5'-r( Cp Cp Cp Cp Cp C)-3'). Chain: a, b, c, d, e, f, g, h, i, j, k, l, m, n, o, p, q, r, s, t. Other_details: non specific RNA from cellular origin bound
Source: Human respiratory syncytial virus a strain long. Organism_taxid: 11260. Expressed in: escherichia coli. Expression_system_taxid: 469008. Escherichia coli. Organism_taxid: 469008. Strain: bl21(de3). Atcc: baa-1025
Resolution:
3.29Å     R-factor:   0.205     R-free:   0.225
Authors: R.G.Tawar,S.Duquerroy,C.Vonrhein,P.F.Varela,L.Damier-Piolle, N.Castagne,K.Maclellan,H.Bedouelle,G.Bricogne,D.Bhella, J.Eleouet,F.A.Rey
Key ref: K.Maclellan et al. (2007). The 24-angstrom structure of respiratory syncytial virus nucleocapsid protein-RNA decameric rings. J Virol, 81, 9519-9524. PubMed id: 17567697
Date:
25-May-09     Release date:   08-Dec-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P03418  (NCAP_HRSVA) -  Nucleoprotein
Seq:
Struc:
391 a.a.
374 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     virion   5 terms 
  Biological process     viral reproduction   5 terms 
  Biochemical function     protein binding     2 terms  

 

 
J Virol 81:9519-9524 (2007)
PubMed id: 17567697  
 
 
The 24-angstrom structure of respiratory syncytial virus nucleocapsid protein-RNA decameric rings.
K.Maclellan, C.Loney, R.P.Yeo, D.Bhella.
 
  ABSTRACT  
 
Respiratory syncytial virus (RSV), a nonsegmented, negative-sense RNA-containing virus, is a common cause of lower respiratory tract disease. Expression of RSV nucleocapsid protein (N) in insect cells using the baculovirus expression system leads to the formation of N-RNA complexes that are morphologically indistinguishable from viral nucleocapsids. When imaged in an electron microscope, three distinct types of structures were observed: tightly wound short-pitch helices, highly extended helices, and rings. Negative stain images of N-RNA rings were used to calculate a three-dimensional reconstruction at 24 A resolution, revealing features similar to those observed in nucleocapsids from other viruses of the order Mononegavirales. The reconstructed N-RNA rings comprise 10 N monomers and have an external radius of 83 A and an internal radius of 40 A. Comparison of this structure with crystallographic data from rabies virus and vesicular stomatitis virus N-RNA rings reveals striking morphological similarities.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19692473 R.Cox, T.J.Green, S.Qiu, J.Kang, J.Tsao, P.E.Prevelige, B.He, and M.Luo (2009).
Characterization of a mumps virus nucleocapsidlike particle.
  J Virol, 83, 11402-11406.  
19965480 R.G.Tawar, S.Duquerroy, C.Vonrhein, P.F.Varela, L.Damier-Piolle, N.Castagné, K.Maclellan, H.Bedouelle, G.Bricogne, D.Bhella, J.F.Eléouët, and F.A.Rey (2009).
Crystal Structure of a Nucleocapsid-Like Nucleoprotein-RNA Complex of Respiratory Syncytial Virus.
  Science, 326, 1279-1283.  
19141448 S.T.Ong, K.Yusoff, C.L.Kho, J.O.Abdullah, and W.S.Tan (2009).
Mutagenesis of the nucleocapsid protein of Nipah virus involved in capsid assembly.
  J Gen Virol, 90, 392-397.  
  18997331 K.El Omari, K.Scott, B.Dhaliwal, J.Ren, N.G.Abrescia, J.Budworth, M.Lockyer, K.L.Powell, A.R.Hawkins, and D.K.Stammers (2008).
Crystallization and preliminary X-ray analysis of the human respiratory syncytial virus nucleocapsid protein.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 1019-1023.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.