Mechanical architecture and folding of E. coli type 1 pilus domains
The pilus type 1 of uropathogenic E. coli must resist mechanical forces to remain attached to the epithelium. Here the authors use single-molecule force spectroscopy to demonstrate a hierarchy of mechanical stability among the pilus domains and show that the oxidoreductase DsbA also acts as a foldin...
Enregistré dans:
| Auteurs principaux: | , , , , , , |
|---|---|
| Format: | article |
| Langue: | EN |
| Publié: |
Nature Portfolio
2018
|
| Sujets: | |
| Accès en ligne: | https://doaj.org/article/90d847fd94ed4db0be96ca5bbf74b922 |
| Tags: |
Ajouter un tag
Pas de tags, Soyez le premier à ajouter un tag!
|
| Résumé: | The pilus type 1 of uropathogenic E. coli must resist mechanical forces to remain attached to the epithelium. Here the authors use single-molecule force spectroscopy to demonstrate a hierarchy of mechanical stability among the pilus domains and show that the oxidoreductase DsbA also acts as a folding chaperone on the domains. |
|---|