Cryo-EM structure of the respiratory syncytial virus RNA polymerase.
Cryoelectron Microscopy
DNA-Directed RNA Polymerases
/ chemistry
Models, Molecular
Phosphoproteins
/ chemistry
Protein Conformation
Protein Domains
RNA-Dependent RNA Polymerase
/ chemistry
Respiratory Syncytial Virus Infections
/ virology
Respiratory Syncytial Virus, Human
/ enzymology
Viral Proteins
/ chemistry
Viral Structures
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
17 01 2020
17 01 2020
Historique:
received:
30
09
2019
accepted:
18
12
2019
entrez:
19
1
2020
pubmed:
19
1
2020
medline:
10
4
2020
Statut:
epublish
Résumé
The respiratory syncytial virus (RSV) RNA polymerase, constituted of a 250 kDa large (L) protein and tetrameric phosphoprotein (P), catalyzes three distinct enzymatic activities - nucleotide polymerization, cap addition, and cap methylation. How RSV L and P coordinate these activities is poorly understood. Here, we present a 3.67 Å cryo-EM structure of the RSV polymerase (L:P) complex. The structure reveals that the RNA dependent RNA polymerase (RdRp) and capping (Cap) domains of L interact with the oligomerization domain (P
Identifiants
pubmed: 31953395
doi: 10.1038/s41467-019-14246-3
pii: 10.1038/s41467-019-14246-3
pmc: PMC6969064
doi:
Substances chimiques
Phosphoproteins
0
Viral Proteins
0
RNA-Dependent RNA Polymerase
EC 2.7.7.48
DNA-Directed RNA Polymerases
EC 2.7.7.6
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
368Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM130950
Pays : United States
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