5E4V

Crystal structure of measles N0-P complex


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.71 Å
  • R-Value Free: 0.266 
  • R-Value Work: 0.211 
  • R-Value Observed: 0.214 

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This is version 1.2 of the entry. See complete history


Literature

Crystal Structure of the Measles Virus Nucleoprotein Core in Complex with an N-Terminal Region of Phosphoprotein.

Guryanov, S.G.Liljeroos, L.Kasaragod, P.Kajander, T.Butcher, S.J.

(2015) J Virol 90: 2849-2857

  • DOI: https://doi.org/10.1128/JVI.02865-15
  • Primary Citation of Related Structures:  
    5E4V

  • PubMed Abstract: 

    The enveloped negative-stranded RNA virus measles virus (MeV) is an important human pathogen. The nucleoprotein (N(0)) assembles with the viral RNA into helical ribonucleocapsids (NC) which are, in turn, coated by a helical layer of the matrix protein. The viral polymerase complex uses the NC as its template. The N(0) assembly onto the NC and the activity of the polymerase are regulated by the viral phosphoprotein (P). In this study, we pulled down an N(0)₁₋₄₀₈ fragment lacking most of its C-terminal tail domain by several affinity-tagged, N-terminal P fragments to map the N(0)-binding region of P to the first 48 amino acids. We showed biochemically and using P mutants the importance of the hydrophobic interactions for the binding. We fused an N(0) binding peptide, P₁₋₄₈, to the C terminus of an N(0)₂₁₋₄₀₈ fragment lacking both the N-terminal peptide and the C-terminal tail of N protein to reconstitute and crystallize the N(0)-P complex. We solved the X-ray structure of the resulting N(0)-P chimeric protein at a resolution of 2.7 Å. The structure reveals the molecular details of the conserved N(0)-P interface and explains how P chaperones N(0), preventing both self-assembly of N(0) and its binding to RNA. Finally, we propose a model for a preinitiation complex for RNA polymerization.


  • Organizational Affiliation

    Institute of Biotechnology, University of Helsinki, Helsinki, Finland.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Nucleoprotein,Phosphoprotein437Measles virus strain Edmonston-BMeasles virus strain Moraten
This entity is chimeric
Mutation(s): 0 
Gene Names: NNP
UniProt
Find proteins for Q77M42 (Measles virus (strain Edmonston-Moraten vaccine))
Explore Q77M42 
Go to UniProtKB:  Q77M42
Find proteins for Q89933 (Measles virus (strain Edmonston B))
Explore Q89933 
Go to UniProtKB:  Q89933
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupsQ89933Q77M42
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.71 Å
  • R-Value Free: 0.266 
  • R-Value Work: 0.211 
  • R-Value Observed: 0.214 
  • Space Group: P 31 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 91.14α = 90
b = 91.14β = 90
c = 94.21γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
PDB_EXTRACTdata extraction
xia2data reduction
xia2data scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Academy of FinlandFinland139178
Academy of FinlandFinland275199
Sigrid Juselius FoundationFinland--
Viikki Doctoral Programme in Molecular BiosciencesFinland--
Biocenter FinlandFinland--
Instruct National affiliate centerFinland--

Revision History  (Full details and data files)

  • Version 1.0: 2016-01-27
    Type: Initial release
  • Version 1.1: 2016-03-09
    Changes: Database references
  • Version 1.2: 2024-01-10
    Changes: Data collection, Database references, Refinement description