7YR8
Lloviu cuevavirus nucleoprotein(1-450 residues)-RNA complex
Summary for 7YR8
Entry DOI | 10.2210/pdb7yr8/pdb |
EMDB information | 34049 |
Descriptor | Nucleoprotein, RNA (5'-R(P*UP*UP*UP*UP*UP*U)-3') (2 entities in total) |
Functional Keywords | nucleoprotein, viral protein |
Biological source | Lloviu cuevavirus More |
Total number of polymer chains | 2 |
Total formula weight | 44989.63 |
Authors | Hu, S.F.,Fujita-Fujiharu, Y.,Sugita, Y.,Wendt, L.,Muramoto, Y.,Nakano, M.,Hoenen, T.,Noda, T. (deposition date: 2022-08-09, release date: 2023-04-19, Last modification date: 2024-07-03) |
Primary citation | Hu, S.,Fujita-Fujiharu, Y.,Sugita, Y.,Wendt, L.,Muramoto, Y.,Nakano, M.,Hoenen, T.,Noda, T. Cryoelectron microscopic structure of the nucleoprotein-RNA complex of the European filovirus, Lloviu virus. Pnas Nexus, 2:pgad120-pgad120, 2023 Cited by PubMed Abstract: Lloviu virus (LLOV) is a novel filovirus detected in Schreiber's bats in Europe. The isolation of the infectious LLOV from bats has raised public health concerns. However, the virological and molecular characteristics of LLOV remain largely unknown. The nucleoprotein (NP) of LLOV encapsidates the viral genomic RNA to form a helical NP-RNA complex, which acts as a scaffold for nucleocapsid formation and de novo viral RNA synthesis. In this study, using single-particle cryoelectron microscopy, we determined two structures of the LLOV NP-RNA helical complex, comprising a full-length and a C-terminally truncated NP. The two helical structures were identical, demonstrating that the N-terminal region determines the helical arrangement of the NP. The LLOV NP-RNA protomers displayed a structure similar to that in the Ebola and Marburg virus, but the spatial arrangements in the helix differed. Structure-based mutational analysis identified amino acids involved in the helical assembly and viral RNA synthesis. These structures advance our understanding of the filovirus nucleocapsid formation and provide a structural basis for the development of antifiloviral therapeutics. PubMed: 37124400DOI: 10.1093/pnasnexus/pgad120 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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