Arg-8 of yeast subunit e contributes to the stability of F-ATP synthase dimers and to the generation of the full-conductance mitochondrial megachannel.
Dimerization
Membrane Potential, Mitochondrial
Mitochondria
/ metabolism
Mitochondrial Membrane Transport Proteins
/ metabolism
Mitochondrial Permeability Transition Pore
Mitochondrial Proton-Translocating ATPases
/ chemistry
Mutagenesis, Site-Directed
Protein Stability
Protein Subunits
/ genetics
Saccharomyces cerevisiae
/ metabolism
Saccharomyces cerevisiae Proteins
/ chemistry
ATP synthase
dimerization
high-conductance channel
megachannel
mitochondria
mitochondrial permeability transition (MPT)
molecular motor
yeast
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
12 07 2019
12 07 2019
Historique:
received:
11
04
2019
revised:
29
05
2019
pubmed:
5
6
2019
medline:
28
2
2020
entrez:
5
6
2019
Statut:
ppublish
Résumé
The mitochondrial F-ATP synthase is a complex molecular motor arranged in V-shaped dimers that is responsible for most cellular ATP synthesis in aerobic conditions. In the yeast F-ATP synthase, subunits e and g of the F
Identifiants
pubmed: 31160339
pii: S0021-9258(20)30197-6
doi: 10.1074/jbc.RA119.008775
pmc: PMC6635451
pii:
doi:
Substances chimiques
Mitochondrial Membrane Transport Proteins
0
Mitochondrial Permeability Transition Pore
0
Protein Subunits
0
Saccharomyces cerevisiae Proteins
0
Mitochondrial Proton-Translocating ATPases
EC 3.6.3.-
Banques de données
PDB
['6B2Z']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
10987-10997Informations de copyright
© 2019 Guo et al.
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