8PZP
Model for influenza A virus helical ribonucleoprotein-like structure
Summary for 8PZP
| Entry DOI | 10.2210/pdb8pzp/pdb |
| Related | 8PZQ |
| EMDB information | 18043 |
| Descriptor | Nucleoprotein, RNA (5'P-(UC)6-FAM3') (2 entities in total) |
| Functional Keywords | influenza virus, nucleocapsid-like, rna binding protein., viral protein |
| Biological source | Influenza A virus (A/WSN/1933(H1N1)) More |
| Total number of polymer chains | 2 |
| Total formula weight | 61149.09 |
| Authors | Chenavier, F.,Estrozi, L.F.,Zarkadas, E.,Ruigrok, R.W.H.,Schoehn, G.,Ballandras-Colas, A.,Crepin, T. (deposition date: 2023-07-27, release date: 2023-12-27) |
| Primary citation | Chenavier, F.,Estrozi, L.F.,Teulon, J.M.,Zarkadas, E.,Freslon, L.L.,Pellequer, J.L.,Ruigrok, R.W.H.,Schoehn, G.,Ballandras-Colas, A.,Crepin, T. Cryo-EM structure of influenza helical nucleocapsid reveals NP-NP and NP-RNA interactions as a model for the genome encapsidation. Sci Adv, 9:eadj9974-eadj9974, 2023 Cited by PubMed Abstract: Influenza virus genome encapsidation is essential for the formation of a helical viral ribonucleoprotein (vRNP) complex composed of nucleoproteins (NP), the trimeric polymerase, and the viral genome. Although low-resolution vRNP structures are available, it remains unclear how the viral RNA is encapsidated and how NPs assemble into the helical filament specific of influenza vRNPs. In this study, we established a biological tool, the RNP-like particles assembled from recombinant influenza A virus NP and synthetic RNA, and we present the first subnanometric cryo-electron microscopy structure of the helical NP-RNA complex (8.7 to 5.3 Å). The helical RNP-like structure reveals a parallel double-stranded conformation, allowing the visualization of NP-NP and NP-RNA interactions. The RNA, located at the interface of neighboring NP protomers, interacts with conserved residues previously described as essential for the NP-RNA interaction. The NP undergoes conformational changes to enable RNA binding and helix formation. Together, our findings provide relevant insights for understanding the mechanism for influenza genome encapsidation. PubMed: 38100595DOI: 10.1126/sciadv.adj9974 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (8.7 Å) |
Structure validation
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