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Encyclopedia of Biophysics pp 129–134Cite as

ATP Synthase Structure

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Synonyms

Complex V; F1Fo-ATP synthase; F-type ATPase; Ion-driven rotary motor; Molecular motors

Definition

Adenosine triphosphate (ATP) synthesizing enzyme by usage of the proton- (sodium-) motive force.

Introduction

Cells need a constant supply of chemically available energy to perform their various cellular activities. Adenosine triphosphate (ATP) is the universal energy supply in all known life forms. This negatively charged compound is impermeable for cell membranes and therefore it needs to be constantly produced by the cell itself. The F1Fo-ATP synthase is a nanosized rotary molecular machine, which produces the bulk supply of ATP. This enzyme is found in mitochondria, chloroplasts, bacteria, and also in the archaeal kingdom (ATP Synthases from Archaea: Structure and Function). The overall architecture of the enzyme comprises two opposing motors, one being the membrane-embedded Fo complex and the other the water-soluble F1 complex (Fig. 1a). The origin of ATP synthases occurred...

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References

  • Abrahams JP, Leslie AGW, Lutter R, Walker JE. Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature. 1994;370:621–8.

    CAS  PubMed  Google Scholar 

  • Boyer PD. The ATP synthase–a splendid molecular machine. Annu Rev Biochem. 1997;66:717–49.

    CAS  PubMed  Google Scholar 

  • Dimroth P. Primary sodium ion translocating enzymes. Biochim Biophys Acta. 1997;1318:11–51.

    CAS  PubMed  Google Scholar 

  • Dmitriev O, Jones PC, Jiang W, Fillingame RH. Structure of the membrane domain of subunit b of the Escherichia coli F0F1 ATP synthase. J Biol Chem. 1999;274:15598–604.

    CAS  PubMed  Google Scholar 

  • Feniouk BA, Yoshida M. Regulatory mechanisms of proton-translocating FoF1-ATP synthase. Results Probl Cell Differ. 2008;45:279–308.

    CAS  PubMed  Google Scholar 

  • Gibbons C, Montgomery MG, Leslie AG, Walker JE. The structure of the central stalk in bovine F1-ATPase at 2.4 Å resolution. Nat Struct Biol. 2000;7:1055–61.

    CAS  PubMed  Google Scholar 

  • Junge W, Sielaff H, Engelbrecht S. Torque generation and elastic power transmission in the rotary FoF1-ATPase. Nature. 2009;459:364–70.

    CAS  PubMed  Google Scholar 

  • Krah A, Pogoryelov D, Langer JD, Bond PJ, Meier T, Faraldo-Gómez JD. Structural and energetic basis for H+ versus Na+ binding selectivity in ATP synthase Fo rotors. Biochim Biophys Acta. 2010;1797:763–772.

    CAS  PubMed  Google Scholar 

  • Lee LK, Stewart AG, Donohoe M, Bernal RA, Stock D. The structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthase. Nat Struct Mol Biol. 2010;17:373–8.

    CAS  PubMed Central  PubMed  Google Scholar 

  • Meier T, Polzer P, Diederichs K, Welte W, Dimroth P. Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus. Science. 2005;308:659–62.

    CAS  PubMed  Google Scholar 

  • Meier T, Krah A, Bond PJ, Pogoryelov D, Diederichs K, Faraldo-Gómez JD. Complete ion-coordination structure in the rotor ring of Na+−dependent F-ATP synthases. J Mol Biol. 2009;391:498–507.

    CAS  PubMed  Google Scholar 

  • Mulkidjanian AY, Makarova KS, Galperin MY, Koonin EV. Inventing the dynamo machine: the evolution of the F-type and V-type ATPases. Nat Rev Microbiol. 2007;5:892–9.

    CAS  PubMed  Google Scholar 

  • Noji H, Yasuda R, Yoshida M, Kinosita Jr K. Direct observation of the rotation of F1-ATPase. Nature. 1997;386:299–302.

    CAS  PubMed  Google Scholar 

  • Pogoryelov D, Yildiz Ö, Faraldo-Gómez JD, Meier T. High-resolution structure of the rotor ring of a proton-dependent ATP synthase. Nat Struct Mol Biol. 2009;16:1068–73.

    CAS  PubMed  Google Scholar 

  • Pogoryelov D, Krah A, Langer JD, Yildiz Ö, Faraldo-Gómez JD, Meier T. Microscopic rotary mechanism of ion translocation in the Fo complex of ATP synthases. Nat Chem Biol. 2010;6:891–9.

    CAS  PubMed  Google Scholar 

  • Preiss L, Yildiz Ö, Hicks DB, Krulwich TA, Meier T. A new type of proton coordination in an F1Fo-ATP synthase rotor ring. PLoS Biol. 2010;8:e000443.

    Google Scholar 

  • Rees DM, Leslie AG, Walker JE. The structure of the membrane extrinsic region of bovine ATP synthase. Proc Natl Acad Sci USA. 2009;106:21597–601.

    CAS  PubMed  Google Scholar 

  • Walker JE, Saraste M, Runswick MJ, Gay NJ. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1982;1:945–51.

    CAS  PubMed  Google Scholar 

  • Wilkens S, Capaldi RA. ATP synthase’s second stalk comes into focus. Nature. 1998;393:29.

    CAS  PubMed  Google Scholar 

  • Wilkens S, Borchardt D, Weber J, Senior AE. Structural characterization of the interaction of the δ and α subunits of the Escherichia coli F1F0-ATP synthase by NMR spectroscopy. Biochemistry. 2005;44:11786–94.

    CAS  PubMed  Google Scholar 

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Author information

Authors and Affiliations

  1. Department of Structural Biology, Max-Planck-Institute of Biophysics, Max-von-Laue-Str. 3, Frankfurt/Main, D-60438, Germany

    Thomas Meier & Denys Pogoryelov

Authors
  1. Thomas Meier
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  2. Denys Pogoryelov
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Corresponding author

Correspondence to Thomas Meier .

Editor information

Editors and Affiliations

  1. Department of Biochemistry, University of Leicester, Leicester, UK

    Gordon C. K. Roberts

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© 2013 European Biophysical Societies' Association (EBSA)

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Meier, T., Pogoryelov, D. (2013). ATP Synthase Structure. In: Roberts, G.C.K. (eds) Encyclopedia of Biophysics. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-16712-6_206

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