Crystal structures of the ATP-binding and ADP-release dwells of the V1 rotary motor

Kano Suzuki; Kenji Mizutani; Shintaro Maruyama; Kazumi Shimono; Fabiana L. Imai; Eiro Muneyuki; Yoshimi Kakinuma; Yoshiko Ishizuka-Katsura; Mikako Shirouzu; Shigeyuki Yokoyama; Ichiro Yamato; Takeshi Murata

doi:10.1038/ncomms13235

Nature Communications (Oct 2016)

Crystal structures of the ATP-binding and ADP-release dwells of the V1 rotary motor

Kano Suzuki,
Kenji Mizutani,
Shintaro Maruyama,
Kazumi Shimono,
Fabiana L. Imai,
Eiro Muneyuki,
Yoshimi Kakinuma,
Yoshiko Ishizuka-Katsura,
Mikako Shirouzu,
Shigeyuki Yokoyama,
Ichiro Yamato,
Takeshi Murata

Affiliations

Kano Suzuki: Department of Chemistry, Graduate School of Science, Chiba University
Kenji Mizutani: Department of Chemistry, Graduate School of Science, Chiba University
Shintaro Maruyama: Department of Chemistry, Graduate School of Science, Chiba University
Kazumi Shimono: Faculty of Pharmaceutical Sciences, Toho University
Fabiana L. Imai: Department of Chemistry, Graduate School of Science, Chiba University
Eiro Muneyuki: Department of Physics, Faculty of Science and Engineering, Chuo University
Yoshimi Kakinuma: Laboratory of Molecular Physiology and Genetics, Faculty of Agriculture, Ehime University
Yoshiko Ishizuka-Katsura: Division of Structural and Synthetic Biology, RIKEN Center for Life Science Technologies
Mikako Shirouzu: Division of Structural and Synthetic Biology, RIKEN Center for Life Science Technologies
Shigeyuki Yokoyama: RIKEN Structural Biology Laboratory
Ichiro Yamato: Department of Biological Science and Technology, Tokyo University of Science
Takeshi Murata: Department of Chemistry, Graduate School of Science, Chiba University

DOI: https://doi.org/10.1038/ncomms13235
Journal volume & issue: Vol. 7, no. 1
pp. 1 – 12

Abstract

Read online

V1-ATPases are rotary molecular motors that are powered by ATP hydrolysis. Here, the authors report two of the missing rotary states of this protein complex, and perform biochemical analysis to investigate the binding mode of the nucleotides.

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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