8CBW

CryoEM structure of the Hendra henipavirus nucleocapsid sauronoid assembly monomer

8CBW の概要

• エントリーDOI: 10.2210/pdb8cbw/pdb
• 関連するPDBエントリー: 8C4H
• EMDBエントリー: 16426
• 分子名称: Nucleocapsid, RNA (5'-R(P*UP*UP*UP*UP*UP*U)-3') (2 entities in total)
• 機能のキーワード: nucleoprotein, rna-binding protein, sauronoid, viral protein
• 由来する生物種: Hendra henipavirus; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60333.36

構造登録者

Passchier, T.C.,Maskell, D.P.,Edwards, T.A.,Barr, J.N. (登録日: 2023-01-26, 公開日: 2024-06-26)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (3.485 Å)