8C4H

CryoEM structure of the Hendra henipavirus nucleocapsid sauronoid assembly multimer

Summary for 8C4H

• Entry DOI: 10.2210/pdb8c4h/pdb
• EMDB information: 16426
• Descriptor: Nucleocapsid, RNA (84-MER) (2 entities in total)
• Functional Keywords: nucleoprotein, rna-binding protein, sauronoid, viral protein
• Biological source: Hendra henipavirus; More
• Total number of polymer chains: 30
• Total formula weight: 1690502.93

Authors

Passchier, T.C.,Maskell, D.P.,Edwards, T.A.,Barr, J.N. (deposition date: 2023-01-04, release date: 2024-06-26)

Primary citation

Passchier, T.C.,White, J.B.R.,Maskell, D.P.,Byrne, M.J.,Ranson, N.A.,Edwards, T.A.,Barr, J.N.
The cryoEM structure of the Hendra henipavirus nucleoprotein reveals insights into paramyxoviral nucleocapsid architectures.
Sci Rep, 14:14099-14099, 2024

PubMed Abstract: We report the first cryoEM structure of the Hendra henipavirus nucleoprotein in complex with RNA, at 3.5 Å resolution, derived from single particle analysis of a double homotetradecameric RNA-bound N protein ring assembly exhibiting D14 symmetry. The structure of the HeV N protein adopts the common bi-lobed paramyxoviral N protein fold; the N-terminal and C-terminal globular domains are bisected by an RNA binding cleft containing six RNA nucleotides and are flanked by the N-terminal and C-terminal arms, respectively. In common with other paramyxoviral nucleocapsids, the lateral interface between adjacent N and N protomers involves electrostatic and hydrophobic interactions mediated primarily through the N-terminal arm and globular domains with minor contribution from the C-terminal arm. However, the HeV N multimeric assembly uniquely identifies an additional protomer-protomer contact between the N N-terminus and N C-terminal arm linker. The model presented here broadens the understanding of RNA-bound paramyxoviral nucleocapsid architectures and provides a platform for further insight into the molecular biology of HeV, as well as the development of antiviral interventions.

PubMed: 38890308
DOI: 10.1038/s41598-024-58243-z

Experimental method

ELECTRON MICROSCOPY (3.485 Å)