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Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F1-Fo coupling.

Murphy BJ, Klusch N, Langer J, Mills DJ, Yildiz Ö, Kühlbrandt W
Science 364 (2019)

Cited: 84 times
EuropePMC logo PMID: 31221832

Abstract

F1Fo-adenosine triphosphate (ATP) synthases make the energy of the proton-motive force available for energy-consuming processes in the cell. We determined the single-particle cryo-electron microscopy structure of active dimeric ATP synthase from mitochondria of Polytomella sp. at a resolution of 2.7 to 2.8 angstroms. Separation of 13 well-defined rotary substates by three-dimensional classification provides a detailed picture of the molecular motions that accompany c-ring rotation and result in ATP synthesis. Crucially, the F1 head rotates along with the central stalk and c-ring rotor for the first ~30° of each 120° primary rotary step to facilitate flexible coupling of the stoichiometrically mismatched F1 and Fo subcomplexes. Flexibility is mediated primarily by the interdomain hinge of the conserved OSCP subunit. A conserved metal ion in the proton access channel may synchronize c-ring protonation with rotation.

Reviews - 6rd4 mentioned but not cited (3)

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  20. The ATPase Inhibitory Factor 1 is a Tissue-Specific Physiological Regulator of the Structure and Function of Mitochondrial ATP Synthase: A Closer Look Into Neuronal Function. Domínguez-Zorita S, Romero-Carramiñana I, Cuezva JM, Esparza-Moltó PB. Front Physiol 13 868820 (2022)
  21. Rotational Mechanism of FO Motor in the F-Type ATP Synthase Driven by the Proton Motive Force. Kubo S, Takada S. Front Microbiol 13 872565 (2022)
  22. F1·Fo ATP Synthase/ATPase: Contemporary View on Unidirectional Catalysis. Zharova TV, Grivennikova VG, Borisov VB. Int J Mol Sci 24 5417 (2023)
  23. Cryo-EM Analyses Permit Visualization of Structural Polymorphism of Biological Macromolecules. Chang WH, Huang SH, Lin HH, Chung SC, Tu IP. Front Bioinform 1 788308 (2021)
  24. Directed proton transfer from Fo to F1 extends the multifaceted proton functions in ATP synthase. Nesterov SV, Yaguzhinsky LS. Biophys Rev 15 859-873 (2023)
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  26. 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)
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Articles citing this publication (51)



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