Structural snapshots of V/A-ATPase reveal the rotary catalytic mechanism of rotary ATPases

V/A-ATPase is a motor protein that shares a common rotary catalytic mechanism with F o F 1 ATP synthase. When powered by ATP hydrolysis, the V 1 domain rotates the central rotor against the A 3 B 3 hexamer, composed of three catalytic AB dimers adopting different conformations (AB open , AB semi , a...

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Bibliographic Details
Published in:	Nature communications Vol. 13; no. 1; p. 1213
Main Authors:	Kishikawa, J., Nakanishi, A., Nakano, A., Saeki, S., Furuta, A., Kato, T., Mistuoka, K., Yokoyama, K.
Format:	Journal Article
Language:	English
Published:	London Nature Publishing Group UK 08-03-2022 Nature Publishing Group Nature Portfolio
Subjects:	101/28 631/45/173 631/45/612/1237 631/535/1258/1259 631/57/1464 82/80 82/83 Adenosine diphosphate Adenosine triphosphatase Adenosine Triphosphatases - metabolism Adenosine Triphosphate - metabolism ATP ATP synthase Binding Dimers Domains Enzymes F1-ATPase FOF1 ATP synthase Humanities and Social Sciences Hydrolysis Intermediates Kinases Models, Molecular Molecular motors multidisciplinary Proteins Proton-Translocating ATPases - metabolism Rotating shafts Rotation Rotors Science Science (multidisciplinary)
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Summary:	V/A-ATPase is a motor protein that shares a common rotary catalytic mechanism with F o F 1 ATP synthase. When powered by ATP hydrolysis, the V 1 domain rotates the central rotor against the A 3 B 3 hexamer, composed of three catalytic AB dimers adopting different conformations (AB open , AB semi , and AB closed ). Here, we report the atomic models of 18 catalytic intermediates of the V 1 domain of V/A-ATPase under different reaction conditions, determined by single particle cryo-EM. The models reveal that the rotor does not rotate immediately after binding of ATP to the V 1 . Instead, three events proceed simultaneously with the 120˚ rotation of the shaft: hydrolysis of ATP in AB semi , zipper movement in AB open by the binding ATP, and unzipper movement in AB closed with release of both ADP and Pi . This indicates the unidirectional rotation of V/A-ATPase by a ratchet-like mechanism owing to ATP hydrolysis in AB semi , rather than the power stroke model proposed previously for F 1 -ATPase. The rotary ATPases use a rotary catalytic mechanism to drive transmembrane proton movement powered by ATP hydrolysis. Here, the authors report a collection of V/A-ATPase V 1 domain structures, providing insights into rotary mechanism of the enzyme and potentially other rotary motor proteins driven by ATP hydrolysis.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	2041-1723 2041-1723
DOI:	10.1038/s41467-022-28832-5