Cryo-EM studies of the rotary H
ATP synthase
V-ATPase
rotary motor
Journal
Biophysics and physicobiology
ISSN: 2189-4779
Titre abrégé: Biophys Physicobiol
Pays: Japan
ID NLM: 101675089
Informations de publication
Date de publication:
2019
2019
Historique:
received:
29
03
2019
accepted:
09
08
2019
entrez:
30
10
2019
pubmed:
30
10
2019
medline:
30
10
2019
Statut:
epublish
Résumé
Proton-translocating rotary ATPases couple proton influx across the membrane domain and ATP hydrolysis/synthesis in the soluble domain through rotation of the central rotor axis against the surrounding peripheral stator apparatus. It is a significant challenge to determine the structure of rotary ATPases due to their intrinsic conformational heterogeneity and instability. Recent progress of single particle analysis of protein complexes using cryogenic electron microscopy (cryo-EM) has enabled the determination of whole rotary ATPase structures and made it possible to classify different rotational states of the enzymes at a near atomic resolution. Three cryo-EM maps corresponding to different rotational states of the V/A type H
Identifiants
pubmed: 31660281
doi: 10.2142/biophysico.16.0_140
pii: 16_140
pmc: PMC6812961
doi:
Types de publication
Journal Article
Review
Langues
eng
Pagination
140-146Informations de copyright
2019 © The Biophysical Society of Japan.
Déclaration de conflit d'intérêts
Conflicts of interest A. N., J. K., K. M., and K. Y declare that they have no conflict of interest.
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