5KND

Crystal structure of the Pi-bound V1 complex

5KND の概要

• エントリーDOI: 10.2210/pdb5knd/pdb
• 関連するPDBエントリー: 5KNB 5KNC
• 分子名称: V-type sodium ATPase catalytic subunit A, V-type sodium ATPase subunit B, V-type sodium ATPase subunit D, ... (9 entities in total)
• 機能のキーワード: p-loop, hydrolase, na(+)-atpase, atp binding
• 由来する生物種: Enterococcus hirae ATCC 9790; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 392692.36

構造登録者

Suzuki, K.,Mizutani, K.,Maruyama, S.,Shimono, K.,Imai, F.L.,Muneyuki, E.,Kakinuma, Y.,Ishizuka-Katsura, Y.,Shirouzu, M.,Yokoyama, S.,Yamato, I.,Murata, T. (登録日: 2016-06-28, 公開日: 2016-11-02, 最終更新日: 2023-11-08)

主引用文献

Suzuki, K.,Mizutani, K.,Maruyama, S.,Shimono, K.,Imai, F.L.,Muneyuki, E.,Kakinuma, Y.,Ishizuka-Katsura, Y.,Shirouzu, M.,Yokoyama, S.,Yamato, I.,Murata, T.
Crystal structures of the ATP-binding and ADP-release dwells of the V1 rotary motor
Nat Commun, 7:13235-13235, 2016

PubMed Abstract: V-ATPases are highly conserved ATP-driven rotary molecular motors found in various membrane systems. We recently reported the crystal structures for the Enterococcus hirae ABDF (V) 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 V 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 V-ATPase rotational mechanism model.

PubMed: 27807367
DOI: 10.1038/ncomms13235

実験手法

X-RAY DIFFRACTION (2.888 Å)