Structural basis of substrate progression through the bacterial chaperonin cycle.
CryoEM
Rubisco
chaperonins
protein folding
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 Dec 2023
12 Dec 2023
Historique:
medline:
8
12
2023
pubmed:
8
12
2023
entrez:
8
12
2023
Statut:
ppublish
Résumé
The bacterial chaperonin GroEL-GroES promotes protein folding through ATP-regulated cycles of substrate protein binding, encapsulation, and release. Here, we have used cryoEM to determine structures of GroEL, GroEL-ADP·BeF
Identifiants
pubmed: 38064510
doi: 10.1073/pnas.2308933120
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2308933120Subventions
Organisme : UKRI | Biotechnology and Biological Sciences Research Council (BBSRC)
ID : BB/M009513/1
Organisme : Wellcome Trust (WT)
ID : 202679/Z/16/Z
Organisme : Wellcome Trust (WT)
ID : 206166/Z/17/Z
Déclaration de conflit d'intérêts
Competing interests statement:M.C.D. was an employee of SPT Labtech, the company that manufactures Chameleon systems.