SNAP output for PDB entry 8ffr [SNAP web server]

PDB-id

8ffr; SNAP-derived features in text and JSON formats; DNAproDB

Class

viral protein

Method

X-ray (3.49 Å)

Summary

Revised structure of the rabies virus nucleoprotein-RNA complex

Reference

Gerard FCA, Bourhis JM, Mas C, Branchard A, Vu DD, Varhoshkova S, Leyrat C, Jamin M (2022): "Structure and Dynamics of the Unassembled Nucleoprotein of Rabies Virus in Complex with Its Phosphoprotein Chaperone Module." Viruses, 14. doi: 10.3390/v14122813.

Abstract

As for all non-segmented negative RNA viruses, rabies virus has its genome packaged in a linear assembly of nucleoprotein (N), named nucleocapsid. The formation of new nucleocapsids during virus replication in cells requires the production of soluble N protein in complex with its phosphoprotein (P) chaperone. In this study, we reconstituted a soluble heterodimeric complex between an armless N protein of rabies virus (RABV), lacking its N-terminal subdomain (N_NT-ARM), and a peptide encompassing the N₀ chaperon module of the P protein. We showed that the chaperone module undergoes a disordered-order transition when it assembles with N₀ and measured an affinity in the low nanomolar range using a competition assay. We solved the crystal structure of the complex at a resolution of 2.3 Å, unveiling the details of the conserved interfaces. MD simulations showed that both the chaperon module of P and RNA-mediated polymerization reduced the ability of the RNA binding cavity to open and close. Finally, by reconstituting a complex with full-length P protein, we demonstrated that each P dimer could independently chaperon two N₀ molecules.