9U6I

Cryo-EM structure of the Vo domain of V/A-ATPase in liposomes, state3

9U6I の概要

• エントリーDOI: 10.2210/pdb9u6i/pdb
• EMDBエントリー: 63909
• 分子名称: V-type ATP synthase subunit I, V-type ATP synthase, subunit K (2 entities in total)
• 機能のキーワード: atp synthase, v atpase, v1 atpase, motor protein
• 由来する生物種: Thermus thermophilus HB8; 詳細
• タンパク質・核酸の鎖数: 13
• 化学式量合計: 122411.96

構造登録者

Nakano, A.,Kishikawa, J.,Nishida, Y.,Shigematsu, H.,Gerle, C.,Mitsuoka, M.,Yokoyama, K. (登録日: 2025-03-23, 公開日: 2025-10-29)

主引用文献

Nakano, A.,Kishikawa, J.I.,Yui, N.,Sugawara, K.,Kan, Y.,Gerle, C.,Shigematsu, H.,Mitsuoka, K.,Yokoyama, K.
Structures of rotary ATP synthase from Thermus thermophilus during proton powered ATP synthesis.
Sci Adv, 11:eadx8771-eadx8771, 2025

PubMed Abstract: ATP synthases are rotary molecular machines that use the proton motive force to rotate the central rotor complex relative to the surrounding stator apparatus, thereby coupling the ATP synthesis. We reconstituted the V/A-ATPase into liposomes and performed structural analysis using cryo-EM under conditions where the proton motive force was applied in the presence of ADP and Pi. ATP molecules were bound at two of the three catalytic sites of V/A-ATPase, confirming that the structure represents a state adopted during ATP synthesis. In this structure, the catalytic site closes upon binding of ADP and Pi through an induced fit mechanism. Multiple structures were obtained where the membrane-embedded rotor ring was in a different position relative to the stator. By comparing these structures, we found that torsion occurs in both the central rotor and the peripheral stator during 31° rotation of rotor ring. These structural snapshots of V/A-ATPase provide crucial insights into the mechanism of rotary catalysis of ATP synthesis.

PubMed: 41105777
DOI: 10.1126/sciadv.adx8771

実験手法

ELECTRON MICROSCOPY (3 Å)