Structural snapshots of V/A-ATPase reveal the rotary catalytic mechanism of rotary ATPases

J. Kishikawa; A. Nakanishi; A. Nakano; S. Saeki; A. Furuta; T. Kato; K. Mistuoka; K. Yokoyama

doi:10.1038/s41467-022-28832-5

Nature Communications (Mar 2022)

Structural snapshots of V/A-ATPase reveal the rotary catalytic mechanism of rotary ATPases

J. Kishikawa,
A. Nakanishi,
A. Nakano,
S. Saeki,
A. Furuta,
T. Kato,
K. Mistuoka,
K. Yokoyama

Affiliations

J. Kishikawa: Department of Molecular Biosciences, Kyoto Sangyo University, Kamigamo-Motoyama
A. Nakanishi: Department of Molecular Biosciences, Kyoto Sangyo University, Kamigamo-Motoyama
A. Nakano: Department of Molecular Biosciences, Kyoto Sangyo University, Kamigamo-Motoyama
S. Saeki: Department of Molecular Biosciences, Kyoto Sangyo University, Kamigamo-Motoyama
A. Furuta: Department of Molecular Biosciences, Kyoto Sangyo University, Kamigamo-Motoyama
T. Kato: Institute for Protein Research, Osaka University
K. Mistuoka: Research Center for Ultra-High Voltage Electron Microscopy, Osaka University
K. Yokoyama: Department of Molecular Biosciences, Kyoto Sangyo University, Kamigamo-Motoyama

DOI: https://doi.org/10.1038/s41467-022-28832-5
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 11

Abstract

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The rotary ATPases use a rotary catalytic mechanism to drive transmembrane proton movement powered by ATP hydrolysis. Here, the authors report a collection of V/A-ATPase V1 domain structures, providing insights into rotary mechanism of the enzyme and potentially other rotary motor proteins driven by ATP hydrolysis.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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