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

<div class='caption-title'>Schematic representation of rotary ATPases and the conventional rotary mechanism.</div>
<div class='caption-title'>Cryo-EM density map and the atomic model for nucleotide-free V/A-ATPase.</div>
<div class='caption-title'>Structures of nucleotide-binding sites obtained in each condition.</div>
Kishikawa J, Nakanishi A, Nakano A, Saeki S, Furuta A, Kato T, Mistuoka K, Yokoyama K
OpenAccess logo Nat Commun 13 1213 (2022)
Related entries: 7vai, 7vaj, 7vak, 7val, 7vam, 7vao, 7vap, 7vaq, 7var, 7vas, 7vat, 7vau, 7vav, 7vaw, 7vax, 7vay, 7vb0

Cited: 12 times
EuropePMC logo PMID: 35260556

Abstract

V/A-ATPase is a motor protein that shares a common rotary catalytic mechanism with FoF1 ATP synthase. When powered by ATP hydrolysis, the V1 domain rotates the central rotor against the A3B3 hexamer, composed of three catalytic AB dimers adopting different conformations (ABopen, ABsemi, and ABclosed). Here, we report the atomic models of 18 catalytic intermediates of the V1 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 V1. Instead, three events proceed simultaneously with the 120˚ rotation of the shaft: hydrolysis of ATP in ABsemi, zipper movement in ABopen by the binding ATP, and unzipper movement in ABclosed 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 ABsemi, rather than the power stroke model proposed previously for F1-ATPase.

Reviews citing this publication (5)

  1. How Does F1-ATPase Generate Torque?: Analysis From Cryo-Electron Microscopy and Rotational Catalysis of Thermophilic F1. Noji H, Ueno H. Front Microbiol 13 904084 (2022)
  2. Visualizing Intramolecular Dynamics of Membrane Proteins. Ohkubo T, Shiina T, Kawaguchi K, Sasaki D, Inamasu R, Yang Y, Li Z, Taninaka K, Sakaguchi M, Fujimura S, Sekiguchi H, Kuramochi M, Arai T, Tsuda S, Sasaki YC, Mio K. Int J Mol Sci 23 14539 (2022)
  3. CryoEM Reveals the Complexity and Diversity of ATP Synthases. Courbon GM, Rubinstein JL. Front Microbiol 13 864006 (2022)
  4. Reversible binding of divalent cations to Ductin protein assemblies-A putative new regulatory mechanism of membrane traffic processes. Sebők-Nagy K, Blastyák A, Juhász G, Páli T. Front Mol Biosci 10 1195010 (2023)
  5. Rotary mechanism of V/A-ATPases-how is ATP hydrolysis converted into a mechanical step rotation in rotary ATPases? Yokoyama K. Front Mol Biosci 10 1176114 (2023)

Articles citing this publication (7)

  1. ClC-7 drives intraphagosomal chloride accumulation to support hydrolase activity and phagosome resolution. Wu JZ, Zeziulia M, Kwon W, Jentsch TJ, Grinstein S, Freeman SA. J Cell Biol 222 e202208155 (2023)
  2. Mechanism of ATP hydrolysis dependent rotation of bacterial ATP synthase. Nakano A, Kishikawa JI, Mitsuoka K, Yokoyama K. Nat Commun 14 4090 (2023)
  3. Direct observation of stepping rotation of V-ATPase reveals rigid component in coupling between Vo and V1 motors. Otomo A, Iida T, Okuni Y, Ueno H, Murata T, Iino R. Proc Natl Acad Sci U S A 119 e2210204119 (2022)
  4. Cryo-EM analysis of V/A-ATPase intermediates reveals the transition of the ground-state structure to steady-state structures by sequential ATP binding. Nakanishi A, Kishikawa JI, Mitsuoka K, Yokoyama K. J Biol Chem 299 102884 (2023)
  5. Editorial Editorial: Functions, working mechanisms, and regulation of rotary ATPases and Ductin proteins. Páli T, Feniouk B, Wilkens S. Front Mol Biosci 11 1399421 (2024)
  6. Participation in 44th Indian Biophysical Society Meeting. Hibino K. Biophys Physicobiol 19 e190033 (2022)
  7. Six states of Enterococcus hirae V-type ATPase reveals non-uniform rotor rotation during turnover. Burton-Smith RN, Song C, Ueno H, Murata T, Iino R, Murata K. Commun Biol 6 755 (2023)


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