The structural basis for inhibition of ribosomal translocation by viomycin.
Anti-Bacterial Agents
/ pharmacology
Crystallography, X-Ray
Escherichia coli
/ drug effects
Models, Molecular
Molecular Conformation
Protein Binding
Protein Biosynthesis
RNA, Messenger
/ genetics
RNA, Ribosomal
/ genetics
RNA, Transfer
/ chemistry
Ribosomal Proteins
/ metabolism
Ribosomes
/ chemistry
Viomycin
/ pharmacology
ribosome
translocation
viomycin
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:
12 05 2020
12 05 2020
Historique:
pubmed:
29
4
2020
medline:
31
7
2020
entrez:
29
4
2020
Statut:
ppublish
Résumé
Viomycin, an antibiotic that has been used to fight tuberculosis infections, is believed to block the translocation step of protein synthesis by inhibiting ribosomal subunit dissociation and trapping the ribosome in an intermediate state of intersubunit rotation. The mechanism by which viomycin stabilizes this state remains unexplained. To address this, we have determined cryo-EM and X-ray crystal structures of
Identifiants
pubmed: 32341159
pii: 2002888117
doi: 10.1073/pnas.2002888117
pmc: PMC7229676
doi:
Substances chimiques
Anti-Bacterial Agents
0
RNA, Messenger
0
RNA, Ribosomal
0
Ribosomal Proteins
0
RNA, Transfer
9014-25-9
Viomycin
YVU35998K5
Banques de données
PDB
['6LKQ', '3KNH', 'EMD-0939']
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
10271-10277Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM118156
Pays : United States
Déclaration de conflit d'intérêts
The authors declare no competing interest.
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