Structure of the vesicular stomatitis virus N⁰-P complex

Replication of non-segmented negative-strand RNA viruses requires the continuous supply of the nucleoprotein (N) in the form of a complex with the phosphoprotein (P). Here, we present the structural characterization of a soluble, heterodimeric complex between a variant of vesicular stomatitis virus...

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Bibliographic Details
Published in:PLoS pathogens 2011-09, Vol.7 (9), p.e1002248-e1002248
Main Authors: Leyrat, Cédric, Yabukarski, Filip, Tarbouriech, Nicolas, Ribeiro, Jr, Euripedes A, Jensen, Malene Ringkjøbing, Blackledge, Martin, Ruigrok, Rob W H, Jamin, Marc
Format: Article
Language:English
Subjects:
Biology
Crystal structure
Crystallography, X-Ray
Experiments
Genomes
Multiprotein Complexes - chemistry
Multiprotein Complexes - genetics
Multiprotein Complexes - metabolism
Nuclear Magnetic Resonance, Biomolecular
Nucleocapsid Proteins - chemistry
Nucleocapsid Proteins - genetics
Nucleocapsid Proteins - metabolism
Peptides
Phosphoproteins - chemistry
Phosphoproteins - genetics
Phosphoproteins - metabolism
Protein Binding
Protein Structure, Quaternary
Proteins
Regulatory Sequences, Ribonucleic Acid - physiology
RNA, Viral - biosynthesis
RNA, Viral - chemistry
RNA, Viral - genetics
Spectrum analysis
Vesiculovirus - chemistry
Vesiculovirus - genetics
Vesiculovirus - metabolism
Viral Structural Proteins - chemistry
Viral Structural Proteins - genetics
Viral Structural Proteins - metabolism
Viruses
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Summary:Replication of non-segmented negative-strand RNA viruses requires the continuous supply of the nucleoprotein (N) in the form of a complex with the phosphoprotein (P). Here, we present the structural characterization of a soluble, heterodimeric complex between a variant of vesicular stomatitis virus N lacking its 21 N-terminal residues (N(Δ21)) and a peptide of 60 amino acids (P(60)) encompassing the molecular recognition element (MoRE) of P that binds RNA-free N (N(0)). The complex crystallized in a decameric circular form, which was solved at 3.0 Å resolution, reveals how the MoRE folds upon binding to N and competes with RNA binding and N polymerization. Small-angle X-ray scattering experiment and NMR spectroscopy on the soluble complex confirms the binding of the MoRE and indicates that its flanking regions remain flexible in the complex. The structure of this complex also suggests a mechanism for the initiation of viral RNA synthesis.
ISSN:1553-7374
1553-7366
1553-7374
DOI:10.1371/journal.ppat.1002248