The cryoEM structure of the Hendra henipavirus nucleoprotein reveals insights into paramyxoviral nucleocapsid architectures.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
18 Jun 2024
18 Jun 2024
Historique:
received:
07
12
2023
accepted:
27
03
2024
medline:
19
6
2024
pubmed:
19
6
2024
entrez:
18
6
2024
Statut:
epublish
Résumé
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
Identifiants
pubmed: 38890308
doi: 10.1038/s41598-024-58243-z
pii: 10.1038/s41598-024-58243-z
doi:
Substances chimiques
Nucleoproteins
0
RNA, Viral
0
Nucleocapsid Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
14099Subventions
Organisme : Horizon 2020 Framework Programme
ID : 721367
Organisme : The Wellcome Trust
ID : 215064/Z/18/Z
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/R00160X/1
Pays : United Kingdom
Informations de copyright
© 2024. The Author(s).
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