Characterizing ATP processing by the AAA+ protein p97 at the atomic level.
Journal
Nature chemistry
ISSN: 1755-4349
Titre abrégé: Nat Chem
Pays: England
ID NLM: 101499734
Informations de publication
Date de publication:
07 Feb 2024
07 Feb 2024
Historique:
received:
24
03
2023
accepted:
04
01
2024
medline:
8
2
2024
pubmed:
8
2
2024
entrez:
7
2
2024
Statut:
aheadofprint
Résumé
The human enzyme p97 regulates various cellular pathways by unfolding hundreds of protein substrates in an ATP-dependent manner, making it an essential component of protein homeostasis and an impactful pharmacological target. The hexameric complex undergoes substantial conformational changes throughout its catalytic cycle. Here we elucidate the molecular motions that occur at the active site in the temporal window immediately before and after ATP hydrolysis by merging cryo-EM, NMR spectroscopy and molecular dynamics simulations. p97 populates a metastable reaction intermediate, the ADP·P
Identifiants
pubmed: 38326645
doi: 10.1038/s41557-024-01440-0
pii: 10.1038/s41557-024-01440-0
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Deutsche Forschungsgemeinschaft (German Research Foundation)
ID : 201302640
Organisme : Deutsche Forschungsgemeinschaft (German Research Foundation)
ID : 201302640
Organisme : Deutsche Forschungsgemeinschaft (German Research Foundation)
ID : 154113120
Organisme : Deutsche Forschungsgemeinschaft (German Research Foundation)
ID : EXC 2067/1-390729940
Organisme : Deutsche Forschungsgemeinschaft (German Research Foundation)
ID : 394455587
Organisme : Deutsche Forschungsgemeinschaft (German Research Foundation)
ID : 201302640
Informations de copyright
© 2024. The Author(s).
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