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ATP synthase — a marvellous rotary engine of the cell

Key Points

  • ATP synthase is a ubiquitous, highly conserved enzyme that catalyses the formation of ATP from ADP and Pi using a unique rotary motor mechanism.

  • The enzyme is located in the inner membrane of mitochondria, in the thylakoid membrane of chloroplasts, and in the plasma membrane of bacteria.

  • Recent analysis of the crystal structure of the enzyme has shown in atomic detail the intricate mechanisms of rotary catalysis.

  • ATP synthase is a large (500 kDa) multisubunit protein, consisting of an intrinsic membrane domain, Fo, linked through central and side stalks to a globular catalytic domain, F1.

  • The F1 portion consists of three α- and three β-subunits and a single γδɛ-subunit, whereas Fo comprises one a-subunit, two b-subunits and 10–12 c-subunits.

  • The synthesis of ATP is brought about by the rotary motion of the FoF1 complex: when a large electrochemical potential (proton gradient) flows through the Fo subunit, this causes rotation of the Fo subunit and, subsequently, F1, leading to ATP synthesis.

  • ATP hydrolysis by ATPase — the reverse reaction — induces rotation of the Fo rotor in the opposite direction. So, ATP synthase can be viewed as a complex of two motors: an ATP-driven F1 motor and the proton-driven Fo motor.

Abstract

ATP synthase can be thought of as a complex of two motors — the ATP-driven F1 motor and the proton-driven Fo motor — that rotate in opposite directions. The mechanisms by which rotation and catalysis are coupled in the working enzyme are now being unravelled on a molecular scale.

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Figure 1: The respiratory chain and ATP synthase.
Figure 2: Structure of ATP synthase.
Figure 3: The crystal structure of mitochondrial F1-ATPase.
Figure 4: Microprobes to detect the rotation of a nano-motor.
Figure 5: Model for the rotary catalysis of ATP synthase.
Figure 6: How many copies of the Foc-subunit are in the ring?
Figure 7: Conformational transition of the ɛ-subunit.

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Acknowledgements

We are grateful to A. Leslie and J. Walker for providing us with the preprint of their paper on the structure of (ADP·AlF4)2F1. We also thank T. Suzuki and K. Tsukuda for their assistance in the preparation of the figures.

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Glossary

ELECTROCHEMICAL POTENTIAL GRADIENT

When two aqueous phases are separated by a membrane, the electrochemical potential difference of H+ between the two phases is expressed as Δ\(\overline{μ}\)H+ = FΔΨ−2.3RTΔpH, where F is the Faraday constant, ΔΨ is the electric potential difference between two phases, R is the gas constant, T is the absolute temperature and ΔpH is pH difference between two phases.

SWITCH II REGION

The β-subunit of F1 has a region that is topologically equivalent to the switch II region of guanine-nucleotide binding (G) proteins, which changes the conformation in response to the interconversion of GTP and GDP.

P-LOOP

Various ATP-metabolizing proteins contain a consensus sequence Gly-X-X-Gly-X-Gly-Lys-Thr (X is variable). This sequence is found in a loop connecting a β-strand (adjacent to a β-strand of switch II region) and an α-helix. The lysine and threonine residues in the P-loop are recruited for binding the phosphate moiety of nucleotides.

V-ATPASE

V-ATPase is responsible for ATP synthesis in archaebacteria and a small number of eubacteria. In eukaryotic cells, it works as a proton-translocating machinery driven by ATP hydrolysis, and it is responsible for the acidification of lysosome lumens, chromaffin granules and vacuoles.

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Yoshida, M., Muneyuki, E. & Hisabori, T. ATP synthase — a marvellous rotary engine of the cell. Nat Rev Mol Cell Biol 2, 669–677 (2001). https://doi.org/10.1038/35089509

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