Principal Investigator


P15  Thomas Meier
Group Leader


Max Planck Institute of Biophysics
Max-von-Laue-Str. 3
60438 Frankfurt am Main, Germany

> publications

P15 Structure and function of bacterial ATP synthases

Ion translocation in the ATP synthase is the culmination point of ATP synthesis in the biological cell. The type of ion that is bound and driving the enzyme is determined and precisely adapted by either the proton- or sodium ion motive force. The ion binding specificity and the number of ions bound to the enzyme’s rotor is hence of central importance for the bioenergetics of the cell. Further, it appears today that the Fo stator subunits represent the last mosaic stone in the collection of high-resolution structures within the oxidative phosphorylation complexes. This assembly of membrane proteins has resisted so far to structural approaches, which have been undertaken in world-leading laboratories in the past decades. Detailed knowledge about the way of ion binding and release from the Fo complex (aim 1) and the molecular assembly and structure of the Fo stator (aim 2) will ultimately contribute to a better understanding of how ion translocation through the Fo complex can cause torque at the enzyme’s rotary subunits and drive the synthesis of ATP. This proposal tackles a central and contemporary question in bioenergetics. It appears that we now have tools at hand that might allow solving the remaining piece in the jigsaw of Mitchell’s revolutionary proposal of energy conversion. 


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).




Preiss L, Langer JD, Yildiz Ö, Eckhardt-Strelau L, Guillemont EG, Koul A, Meier T* (2015) Structure of the mycobacterial ATP synthase Fo rotor ring in complex with the anti-TB drug bedaquiline. Sci Adv 1, e1500106.

Leone V, Pogoryelov D, Meier T, Faraldo-Gómez JD* (2015) On the principle of ion selectivity in Na+/H+-coupled membrane proteins: experimental and theoretical studies of an ATP synthase rotor. Proc Natl Acad Sci USA 112, E1057-66.

Preiss L, Hicks DB, Suzuki S, Meier T*, Krulwich TA (2015) Alkaliphilic bacteria with impact on industrial applications, concepts of early life forms, and bioenergetics of ATP synthesis. Front Bioeng Biotechnol 3, 75.

Matthies D, Zhou W, Klyszejko AL, Anselmi C, Yildiz Ö, Brandt K, Müller V, Faraldo-Gómez JD*, Meier T* (2014) High-resolution structure and mechanism of an F/V-hybrid rotor ring in a Na+-coupled ATP synthase. Nat Commun 5, 5286.

Preiss L, Langer JD, Hicks DB, Liu J, Yildiz Ö, Krulwich TA, Meier T* (2014) The c-ring ion-binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic lifestyle. Mol Microbiol 92, 973-84.

Preiss L, Klyszejko AL, Hicks DB, Liu J, Fackelmayer OJ, Yildiz Ö, Krulwich TA, Meier T* (2013) The c-ring stoichiometry of ATP synthase is adapted to cell physiological requirements of alkaliphilic Bacilllus pseudofirmus OF4. Proc Natl Acad Sci USA 110, 7874-9.

Schulz S, Iglesias-Cans M, Krah A, Yildiz Ö, Leone V, Matthies D, Cook GM, Faraldo-Gómez JD, Meier T* (2013) A new type of Na+-driven ATP synthase membrane rotor with a two-carboxylate ion-coupling motif. PLoS Biology 11, e1001596.

Halang P, Leptihn S, Meier T, Vorburger T*, Steuber J* (2013) The function of the Na+-driven flagellum of Vibrio cholerae is determined by osmolality and pH. J Bacteriol 95, 4888-99.

Meier T*, Pogoryelov D (2013) ATP synthase structure. Roberts G (Ed) Encyclopedia of Biophysics, Springer-Verlag Berlin Heidelberg 1, 129-34.

*corresponding author





Müller (P14), Kühlbrandt (P1), Michel (P3)