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

Nature Communications, 2016, vol. 7, issue 1, 1-12

Abstract: Abstract V1-ATPases are highly conserved ATP-driven rotary molecular motors found in various membrane systems. We recently reported the crystal structures for the Enterococcus hirae A3B3DF (V1) complex, corresponding to the catalytic dwell state waiting for ATP hydrolysis. Here we present the crystal structures for two other dwell states obtained by soaking nucleotide-free V1 crystals in ADP. In the presence of 20 μM ADP, two ADP molecules bind to two of three binding sites and cooperatively induce conformational changes of the third site to an ATP-binding mode, corresponding to the ATP-binding dwell. In the presence of 2 mM ADP, all nucleotide-binding sites are occupied by ADP to induce conformational changes corresponding to the ADP-release dwell. Based on these and previous findings, we propose a V1-ATPase rotational mechanism model.

Date: 2016
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DOI: 10.1038/ncomms13235

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