Structure of a Tc holotoxin pore provides insights into the translocation mechanism.
Photorhabdus
Tc
cryo-EM
toxin
translocation
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 11 2019
12 11 2019
Historique:
pubmed:
2
11
2019
medline:
2
4
2020
entrez:
1
11
2019
Statut:
ppublish
Résumé
Tc toxins are modular toxin systems of insect and human pathogenic bacteria. They are composed of a 1.4-MDa pentameric membrane translocator (TcA) and a 250-kDa cocoon (TcB and TcC) encapsulating the 30-kDa toxic enzyme (C terminus of TcC). Binding of Tc toxins to target cells and a pH shift trigger the conformational transition from the soluble prepore state to the membrane-embedded pore. Subsequently, the toxic enzyme is translocated and released into the cytoplasm. A high-resolution structure of a holotoxin embedded in membranes is missing, leaving open the question of whether TcB-TcC has an influence on the conformational transition of TcA. Here we show in atomic detail a fully assembled 1.7-MDa Tc holotoxin complex from
Identifiants
pubmed: 31666324
pii: 1909821116
doi: 10.1073/pnas.1909821116
pmc: PMC6859359
doi:
Substances chimiques
Bacterial Toxins
0
ADP Ribose Transferases
EC 2.4.2.-
Banques de données
PDB
['6SUE', '6SUF']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Video-Audio Media
Langues
eng
Sous-ensembles de citation
IM
Pagination
23083-23090Déclaration de conflit d'intérêts
The authors declare no competing interest.
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