Structure of the Vesicular Stomatitis Virus L Protein in Complex with Its Phosphoprotein Cofactor.
antiviral
ebola
polymerase
rabies
respiratory syncytial virus
rhabdoviruses
Journal
Cell reports
ISSN: 2211-1247
Titre abrégé: Cell Rep
Pays: United States
ID NLM: 101573691
Informations de publication
Date de publication:
07 01 2020
07 01 2020
Historique:
received:
02
10
2019
revised:
22
11
2019
accepted:
06
12
2019
entrez:
9
1
2020
pubmed:
9
1
2020
medline:
7
1
2021
Statut:
ppublish
Résumé
The large (L) proteins of non-segmented, negative-strand RNA viruses are multifunctional enzymes that produce capped, methylated, and polyadenylated mRNA and replicate the viral genome. A phosphoprotein (P), required for efficient RNA-dependent RNA polymerization from the viral ribonucleoprotein (RNP) template, regulates the function and conformation of the L protein. We report the structure of vesicular stomatitis virus L in complex with its P cofactor determined by electron cryomicroscopy at 3.0 Å resolution, enabling us to visualize bound segments of P. The contacts of three P segments with multiple L domains show how P induces a closed, compact, initiation-competent conformation. Binding of P to L positions its N-terminal domain adjacent to a putative RNA exit channel for efficient encapsidation of newly synthesized genomes with the nucleoprotein and orients its C-terminal domain to interact with an RNP template. The model shows that a conserved tryptophan in the priming loop can support the initiating 5' nucleotide.
Identifiants
pubmed: 31914397
pii: S2211-1247(19)31674-2
doi: 10.1016/j.celrep.2019.12.024
pmc: PMC7049099
mid: NIHMS1548558
pii:
doi:
Substances chimiques
Coenzymes
0
Phosphoproteins
0
Protein Subunits
0
Viral Proteins
0
L protein, vesicular stomatitis virus
EC 2.7.7.48
RNA-Dependent RNA Polymerase
EC 2.7.7.48
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
53-60.e5Subventions
Organisme : NIAID NIH HHS
ID : R37 AI059371
Pays : United States
Organisme : Howard Hughes Medical Institute
Pays : United States
Informations de copyright
Copyright © 2019 The Authors. Published by Elsevier Inc. All rights reserved.
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