An affinity change model to elucidate the rotation mechanism of V
Affinity
Central shaft rotation
Crystal structure
Surface plasmon resonance
Thermal fluctuation
V(1)-ATPase
Journal
Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516
Informations de publication
Date de publication:
17 12 2020
17 12 2020
Historique:
received:
30
09
2020
accepted:
13
10
2020
pubmed:
25
10
2020
medline:
26
3
2021
entrez:
24
10
2020
Statut:
ppublish
Résumé
V-ATPases are ubiquitous proton-transporting ATPases of eukaryotic and prokaryotic membranes that utilize energy from ATP hydrolysis. The hydrophilic catalytic part called V
Identifiants
pubmed: 33097182
pii: S0006-291X(20)31948-3
doi: 10.1016/j.bbrc.2020.10.033
pii:
doi:
Substances chimiques
Protein Subunits
0
Recombinant Fusion Proteins
0
Adenosine Diphosphate
61D2G4IYVH
Adenosine Triphosphate
8L70Q75FXE
Vacuolar Proton-Translocating ATPases
EC 3.6.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1413-1418Informations de copyright
Copyright © 2020 Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interests The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.