Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
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Journal
IF	>30 >20 >10 >5 all

Title	Structure of the tilapia lake virus nucleoprotein bound to RNA.
Journal, issue, pages	Nucleic Acids Res, Vol. 53, Issue 4, Year 2025
Publish date	Feb 8, 2025
Authors	Benoît Arragain / Martin Pelosse / Karine Huard / Stephen Cusack /
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, ...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.
External links	Nucleic Acids Res / PubMed:39995042 / PubMed Central
Methods	EM (single particle)
Resolution	2.9 - 3.68 Å
Structure data	52027 9hbr EMDB-52027, PDB-9hbr: TiLV-NP pentamer (pseudo-C5) (local refinement around 2 TiLV-NPs) Method: EM (single particle) / Resolution: 2.9 Å 52028 9hbs EMDB-52028, PDB-9hbs: TiLV-NP tetramer (pseudo-C2) Method: EM (single particle) / Resolution: 3.68 Å 52029 9hbt EMDB-52029, PDB-9hbt: TiLV-NP pentamer (pseudo-C5) Method: EM (single particle) / Resolution: 3.46 Å 52030 9hbu EMDB-52030, PDB-9hbu: TiLV-NP tetramer (pseudo-C2) (local refinement around 2 TiLV-NPs) Method: EM (single particle) / Resolution: 3.51 Å 52031 9hbv EMDB-52031, PDB-9hbv: TiLV-NP tetramer (pseudo-C4) (local refinement around 2 TiLV-NPs) Method: EM (single particle) / Resolution: 3.38 Å 52032 9hbw EMDB-52032, PDB-9hbw: TiLV-NP tetramer (pseudo-C4) Method: EM (single particle) / Resolution: 3.59 Å 52033 9hbx EMDB-52033, PDB-9hbx: TiLV-NP hexamer (pseudo-C6) (local refinement around 2 TiLV-NPs) Method: EM (single particle) / Resolution: 3.04 Å 52034 9hby EMDB-52034, PDB-9hby: TiLV-NP hexamer (pseudo-C6) (local refinement around 3 TiLV-NPs) Method: EM (single particle) / Resolution: 3.1 Å 52035 9hbz EMDB-52035, PDB-9hbz: TiLV-NP hexamer (pseudo-C6) Method: EM (single particle) / Resolution: 3.49 Å
Source	tilapia lake virus
Keywords	RNA BINDING PROTEIN / Viral protein / nucleoprotein / oligomer