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

Content Provider	Semantic Scholar
Author	Suzuki, Kazuya Z. Mizutani, Kenji Maruyama, Shintaro Shimono, Kaneyoshi Imai, Fabiana Lica Muneyuki, Eiro Kakinuma, Yoshimi Ishizuka-Katsura, Yoshiko Shirouzu, Mikako Yokoyama, Shigeyuki Yamato, Ichiro Murata, Takeshi
Copyright Year	2016
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.
Starting Page	1
Ending Page	16
Page Count	16
File Format	PDF HTM / HTML
PubMed reference number	27807367v1
Alternate Webpage(s)	https://doi.org/10.1038/ncomms13235
DOI	10.1038/ncomms13235
Journal	Nature communications
Volume Number	7
Language	English
Access Restriction	Open
Subject Keyword	Adenosine Diphosphate Adenosine Triphosphate Binding Sites Nucleotides Tissue membrane
Content Type	Text
Resource Type	Article