8B8V
Crystal structure of the Rabies virus RNA free nucleoprotein- phosphoprotein complex
Summary for 8B8V
| Entry DOI | 10.2210/pdb8b8v/pdb |
| Descriptor | Nucleoprotein, Phosphoprotein, DI(HYDROXYETHYL)ETHER, ... (4 entities in total) |
| Functional Keywords | chaperone, complex, replication machinery, virus, viral protein |
| Biological source | Lyssavirus rabies More |
| Total number of polymer chains | 2 |
| Total formula weight | 56817.80 |
| Authors | Gerard, F.C.A.,Jamin, M.,Bourhis, J.M. (deposition date: 2022-10-05, release date: 2023-03-15, Last modification date: 2024-02-07) |
| Primary citation | Gerard, F.C.A.,Bourhis, J.M.,Mas, C.,Branchard, A.,Vu, D.D.,Varhoshkova, S.,Leyrat, C.,Jamin, M. Structure and Dynamics of the Unassembled Nucleoprotein of Rabies Virus in Complex with Its Phosphoprotein Chaperone Module. Viruses, 14:-, 2022 Cited by PubMed 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), and a peptide encompassing the N chaperon module of the P protein. We showed that the chaperone module undergoes a disordered-order transition when it assembles with N 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 N molecules. PubMed: 36560817DOI: 10.3390/v14122813 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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