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
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

140-146

Informations 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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Auteurs

Atsuko Nakanishi (A)

Department of Molecular Biosciences, Kyoto Sangyo University, Kyoto 603-8555, Japan.

Jun-Ichi Kishikawa (JI)

Department of Molecular Biosciences, Kyoto Sangyo University, Kyoto 603-8555, Japan.

Kaoru Mitsuoka (K)

Research Center for Ultra-High Voltage Electron Microscopy, Osaka University, Ibaraki, Osaka 567-0047 Japan.

Ken Yokoyama (K)

Department of Molecular Biosciences, Kyoto Sangyo University, Kyoto 603-8555, Japan.

Classifications MeSH