9HBW
TiLV-NP tetramer (pseudo-C4)
Summary for 9HBW
| Entry DOI | 10.2210/pdb9hbw/pdb |
| EMDB information | 52032 |
| Descriptor | Tilapia Lake Virus nucleoprotein (segment 4), 40-mer vRNA loop (3 entities in total) |
| Functional Keywords | viral protein, nucleoprotein, oligomer, rna binding protein |
| Biological source | Tilapia lake virus More |
| Total number of polymer chains | 8 |
| Total formula weight | 170717.61 |
| Authors | |
| Primary citation | Arragain, B.,Pelosse, M.,Huard, K.,Cusack, S. Structure of the tilapia lake virus nucleoprotein bound to RNA. Nucleic Acids Res., 53:-, 2025 Cited by PubMed Abstract: Tilapia Lake virus (TiLV) belongs to the Amnoonviridae family within the Articulavirales order of segmented negative-strand RNA viruses and is highly diverged from more familiar orthomyxoviruses, such as influenza. The viral nucleoprotein (NP), a key component of the replication machinery, packages the viral genome into protective ribonucleoprotein particles. Here we describe the electron cryo-microscopy (cryo-EM) structure of TiLV-NP bound to RNA within in vitro reconstituted, small ring-like, pseudo-symmetrical oligomers. Although TiLV-NP is considerably smaller than its influenza counterpart and unrelated in sequence, it maintains the same topology and domain organisation. This comprises a head and body domain between which is a positively charged groove, where single-stranded RNA binds. In addition, an oligomerisation loop inserts into a hydrophobic pocket in the neighbouring NP, the flexible hinges of which allow variable orientation of adjacent NPs. Focused cryo-EM maps unambiguously define the 5' to 3' direction of the bound RNA, confirmed by double stranded, A-form RNA regions that extrude out from some of the NP-NP interfaces. This is the first fully resolved description of how single-stranded and stem-loop RNA binds to an articulaviral NP assembly. Superposition with orthomyxoviral NPs suggest that the mode of RNA binding is likely similar across the Articulavirales order. PubMed: 39995042DOI: 10.1093/nar/gkaf112 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.59 Å) |
Structure validation
Download full validation report
