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

• DOI: 10.1038/ncomms13235
• Publication Date: 2016-10-27T10:16:54Z
• Authors: Kano Suzuki; Kenji Mizutani; Shintaro Maruyama; Kazumi Shimono; Fabiana L. Imai; Eiro Muneyuki; Yoshimi Kakinuma; Yoshiko Ishizuka-...; Mikako Shirouzu; Shigeyuki Yokoyama; Ichiro Yamato; Takeshi Murata
• Keywords: Molecular motor; Adenosine triphosphate; Dwell time

Abstract V 1 -ATPases are highly conserved ATP-driven rotary molecular motors found in various membrane systems. We recently reported the crystal structures for Enterococcus hirae A 3 B DF (V ) complex, corresponding to catalytic dwell state waiting ATP hydrolysis. Here we present two other states obtained by soaking nucleotide-free crystals ADP. In presence of 20 μM ADP, ADP molecules bind three binding sites and cooperatively induce conformational changes third site an ATP-binding mode, dwell. 2 mM all nucleotide-binding occupied ADP-release Based on these previous findings, propose a -ATPase rotational mechanism model.