Structural basis of the monkeypox virus mRNA cap N7 methyltransferase complex.
Monkeypox virus
SAXS
mRNA cap N7 methyltransferase
protein complex
structure
Journal
Emerging microbes & infections
ISSN: 2222-1751
Titre abrégé: Emerg Microbes Infect
Pays: United States
ID NLM: 101594885
Informations de publication
Date de publication:
Dec 2024
Dec 2024
Historique:
medline:
27
6
2024
pubmed:
14
6
2024
entrez:
14
6
2024
Statut:
ppublish
Résumé
The global outbreak of Mpox, caused by the monkeypox virus (MPXV), has attracted international attention and become another major infectious disease event after COVID-19. The mRNA cap N7 methyltransferase (RNMT) of MPXV methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs and plays a vital role in evading host antiviral immunity. MPXV RNMT is composed of the large subunit E1 and the small subunit E12. How E1 and E12 of MPXV assembly remains unclear. Here, we report the crystal structures of E12, the MTase domain of E1 with E12 (E1
Identifiants
pubmed: 38873898
doi: 10.1080/22221751.2024.2369193
doi:
Substances chimiques
Methyltransferases
EC 2.1.1.-
Viral Proteins
0
RNA Caps
0
RNA, Messenger
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM