Principal Investigator
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P15 Thomas Meier
Group Leader
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Max Planck Institute of Biophysics
Max-von-Laue-Str. 3
60438 Frankfurt am Main, Germany
Phone +49 (0)69 6303-3038
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P15 Structure and function of bacterial F-ATP synthases
F1Fo-ATP synthase uses the ion gradient created by the respiratory chain complexes to form adenosine triphosphate (ATP) by a unique rotary mechanism. Whereas in the F1 complex ADP and Pi is converted into ATP, the Fo complex translocates ions across the energized membrane which results in torque generation at the rotor part of the enzyme. In bacteria the Fo contains the subunits ab2c10-15. For a yet unknown reason, the c oligomers seem to have a fixed stoichiometry within one defined species but are variable among different species. This variance is meaningful; it has a direct impact on the ‘ion-to-ATP-ratio’ of the enzyme and hence bioenergetic efficacy of the cell. For a clearer understanding of how the ATP synthase works, structural information about the stator subunit a in the Fo part and its interaction with the rotary c-ring is needed. In our work about ATP synthases we therefore focus on the two questions:
1) How does ion translocation through Fo induce torque at the rotor-stator interface?
2) What factors determine the c-ring stoichiometry in the Fo complex and why is it variable among the species?
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- Figure 1. Model of a bacterial ATP synthase incorporated into a membrane (Ref. 3, with kind permission of NPG (Nature Publishing Group, London).
Movie 1.
The rotating Ilyobacter tartaricus c11 ring (Ref. 5).
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Publications
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Pogoryelov, D., Krah, A., Langer, J.D., Yildiz, Ö., Faraldo-Gómez, J.D. and Meier, T. (2010) Microscopic rotary mechanism of ion translocation in the Fo complex of ATP synthases. Nat Chem Biol 6, 891-899.
Preiss, L., Yildiz, Ö., Hicks, D.B., Krulwich, T.A. and Meier, T. (2010) A new type of proton coordination in an F1Fo-ATP synthase rotor ring. PLoS Biology 8, e1000443.
Pogoryelov, D,, Yildiz, Ö., Faraldo-Gómez, J.D. and Meier, T. (2009) High-resolution structure of the rotor ring of a proton-dependent ATP synthase. Nat Struct Mol Biol 16, 1068-1073.
Matthies, D., Preiss, L., Klyszejko, A.L., Muller, D.J., Cook, G.M., Vonck, J. and Meier, T. (2009) The c13 ring from a thermoalkaliphilic ATP synthase reveals an extended diameter due to a special structural region. J Mol Biol 388, 611-618.
Meier, T., Krah, A., Bond, P.J., Pogoryelov, D., Diederichs, K. and Faraldo-Gómez, J.D. (2009) Complete ion-coordination structure in the rotor ring of Na+-dependent F-ATP synthases. J Mol Biol 391, 498-507.
Pogoryelov, D., Nikolaev, Y., Schlattner, U., Pervushin, K., Dimroth, P. and Meier, T. (2008) Probing the rotor subunit interface of the ATP synthase from Ilyobacter tartaricus. FEBS J 275, 4850-4862