9GAV
Focused reconstruction on strand 1 of the influenza A RNP-like particle double-stranded assembled with a 18-mer RNA.
This is a non-PDB format compatible entry.
Summary for 9GAV
| Entry DOI | 10.2210/pdb9gav/pdb |
| EMDB information | 51184 51185 51186 51187 51188 51189 |
| Descriptor | Nucleoprotein, RNA (5'-P(UC)9-FAM3'), 2-[3,6-bis(oxidanylidene)-4,5-dihydroxanthen-9-yl]-4-[3-[(2R)-2-oxidanylpropoxy]propylcarbamoyl]benzoic acid (3 entities in total) |
| Functional Keywords | nucleoprotein, rna, complex, rnp-like, influenza virus, viral protein |
| Biological source | Influenza A virus More |
| Total number of polymer chains | 6 |
| Total formula weight | 185809.71 |
| Authors | Chenavier, F.,Ruigrok, R.W.H.,Schoehn, G.,Ballandras-Colas, A.,Crepin, T. (deposition date: 2024-07-29, release date: 2025-01-15, Last modification date: 2025-02-12) |
| Primary citation | Chenavier, F.,Zarkadas, E.,Freslon, L.L.,Stelfox, A.J.,Schoehn, G.,Ruigrok, R.W.H.,Ballandras-Colas, A.,Crepin, T. Influenza a virus antiparallel helical nucleocapsid-like pseudo-atomic structure. Nucleic Acids Res., 53:-, 2025 Cited by PubMed Abstract: Influenza A viruses are responsible for human seasonal epidemics and severe animal pandemics with a risk of zoonotic transmission to humans. The viral segmented RNA genome is encapsidated by nucleoproteins (NP) and attached to the heterotrimeric polymerase, forming the viral ribonucleoproteins (vRNPs). Flexible helical vRNPs are central for viral transcription and replication. In this study, we present an advanced biological tool, the antiparallel helical RNP-like complex, assembled from recombinant N-terminally truncated NP and short synthetic RNA. The 3.0 Å cryo-electron microscopy structure details for the first time the whole RNA pathway across NP as well as NP-NP interactions that drive the antiparallel helical assembly accommodating major and minor grooves. Our findings show that the surface of the protein can harbour several conformations of the RNA, confirming that the number of nucleobases that binds to NP is not fixed, but ranges probably between 20 and 24. Taking all together, our data provide details to further understand the genome encapsidation and explain the inherent flexibility of influenza A virus vRNPs. PubMed: 39673795DOI: 10.1093/nar/gkae1211 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.04 Å) |
Structure validation
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