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Biochemical and electron microscopic characterization of the F1F0 ATP Synthase from the hyperthermophilic eubacterium Aquifex aeolicus

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Peng,  Guohong
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;
Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266071, China;

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Bostina,  Mihnea
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Michel,  Hartmut
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Peng, G., Bostina, M., Radermacher, M., Rais, I., Karas, M., & Michel, H. (2006). Biochemical and electron microscopic characterization of the F1F0 ATP Synthase from the hyperthermophilic eubacterium Aquifex aeolicus. FEBS Letters, 580(25), 5934-5940. doi:10.1016/j.febslet.2006.09.062.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-D9B2-7
Abstract
The F1F0 ATP synthase has been purified from the hyperthermophilic eubacterium Aquifex aeolicus and characterized. Its subunits have been identified by MALDI-mass spectrometry through peptide mass fingerprinting and MS/MS. It contains the canonical subunits alpha, beta, gamma, delta and epsilon of F1 and subunits a and c of F0. Two versions of the b subunit were found, which show a low sequence homology to each other. Most likely they form a heterodimer. An electron microscopic single particle analysis revealed clear structural details, including two stalks connecting F1 and F0. In several orientations the central stalk appears to be tilted and/or kinked. It is unclear whether there is a direct connection between the peripheral stalk and the delta subunit.