Structural insights into RNA recognition by the Chikungunya virus nsP2 helicase.
ATP hydrolysis
Alphavirus
Chikungunya virus
nonstructural protein 2
superfamily 1 helicase
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
07 05 2019
07 05 2019
Historique:
pubmed:
20
4
2019
medline:
17
3
2020
entrez:
20
4
2019
Statut:
ppublish
Résumé
Chikungunya virus (CHIKV) is transmitted to humans through mosquitoes and causes Chikungunya fever. Nonstructural protein 2 (nsP2) exhibits the protease and RNA helicase activities that are required for viral RNA replication and transcription. Unlike for the C-terminal protease, the structure of the N-terminal RNA helicase (nsP2h) has not been determined. Here, we report the crystal structure of the nsP2h bound to the conserved 3'-end 14 nucleotides of the CHIKV genome and the nonhydrolyzable transition-state nucleotide analog ADP-AlF
Identifiants
pubmed: 31000599
pii: 1900656116
doi: 10.1073/pnas.1900656116
pmc: PMC6511008
doi:
Substances chimiques
Organometallic Compounds
0
RNA, Viral
0
Viral Proteins
0
adenosine diphosphate tetrafluoroaluminate
0
Adenosine Diphosphate
61D2G4IYVH
RNA Helicases
EC 3.6.4.13
Banques de données
PDB
['6JIM']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
9558-9567Déclaration de conflit d'intérêts
The authors declare no conflict of interest.
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