7UWS
Atomic model of the partial VSV nucleocapsid
Summary for 7UWS
| Entry DOI | 10.2210/pdb7uws/pdb |
| EMDB information | 26841 |
| Descriptor | Nucleoprotein, RNA, Matrix protein (3 entities in total) |
| Functional Keywords | vesicular stomatitis virus, nucleocapsid, matrix protein m, nucleocapsid protein n, viral protein-rna complex, viral protein/rna |
| Biological source | Vesicular stomatitis virus More |
| Total number of polymer chains | 20 |
| Total formula weight | 763589.78 |
| Authors | |
| Primary citation | Zhou, K.,Si, Z.,Ge, P.,Tsao, J.,Luo, M.,Zhou, Z.H. Atomic model of vesicular stomatitis virus and mechanism of assembly. Nat Commun, 13:5980-5980, 2022 Cited by PubMed Abstract: Like other negative-strand RNA viruses (NSVs) such as influenza and rabies, vesicular stomatitis virus (VSV) has a three-layered organization: a layer of matrix protein (M) resides between the glycoprotein (G)-studded membrane envelope and the nucleocapsid, which is composed of the nucleocapsid protein (N) and the encapsidated genomic RNA. Lack of in situ atomic structures of these viral components has limited mechanistic understanding of assembling the bullet-shaped virion. Here, by cryoEM and sub-particle reconstruction, we have determined the in situ structures of M and N inside VSV at 3.47 Å resolution. In the virion, N and M sites have a stoichiometry of 1:2. The in situ structures of both N and M differ from their crystal structures in their N-terminal segments and oligomerization loops. N-RNA, N-N, and N-M-M interactions govern the formation of the capsid. A double layer of M contributes to packaging of the helical nucleocapsid: the inner M (IM) joins neighboring turns of the N helix, while the outer M (OM) contacts G and the membrane envelope. The pseudo-crystalline organization of G is further mapped by cryoET. The mechanism of VSV assembly is delineated by the network interactions of these viral components. PubMed: 36216930DOI: 10.1038/s41467-022-33664-4 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.47 Å) |
Structure validation
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