5E4V

Crystal structure of measles N0-P complex

Summary for 5E4V

• Entry DOI: 10.2210/pdb5e4v/pdb
• Descriptor: Nucleoprotein,Phosphoprotein (2 entities in total)
• Functional Keywords: paramyxovirus, nucleocapsid protein, rna-binding protein, viral protein
• Biological source: Measles virus (strain Edmonston B) (MeV); More
• Total number of polymer chains: 1
• Total formula weight: 48446.99

Authors

Guryanov, S.G.,Liljeroos, L.,Kasaragod, P.,Kajander, T.,Butcher, S.J. (deposition date: 2015-10-07, release date: 2016-01-27, Last modification date: 2024-01-10)

Primary citation

Guryanov, S.G.,Liljeroos, L.,Kasaragod, P.,Kajander, T.,Butcher, S.J.
Crystal Structure of the Measles Virus Nucleoprotein Core in Complex with an N-Terminal Region of Phosphoprotein.
J.Virol., 90:2849-2857, 2015

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.

PubMed: 26719278
DOI: 10.1128/JVI.02865-15

Experimental method

X-RAY DIFFRACTION (2.71 Å)