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Structure of the c10 ring of the yeast mitochondrial ATP synthase in the open conformation

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Krah,  Alexander
Max Planck Research Group of Theoretical Molecular Biophysics, Max Planck Institute of Biophysics, Max Planck Society;

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Meier,  Thomas
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Faraldo-Gómez,  José D.
Max Planck Research Group of Theoretical Molecular Biophysics, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Symersky, J., Pagadala, V., Osowski, D., Krah, A., Meier, T., Faraldo-Gómez, J. D., et al. (2012). Structure of the c10 ring of the yeast mitochondrial ATP synthase in the open conformation. Nature Structural and Molecular Biology, 19, 485-491. doi:10.1038/nsmb.2284.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-D5B3-3
Abstract
The proton pore of the F(1)F(o) ATP synthase consists of a ring of c subunits, which rotates, driven by downhill proton diffusion across the membrane. An essential carboxylate side chain in each subunit provides a proton-binding site. In all the structures of c-rings reported to date, these sites are in a closed, ion-locked state. Structures are here presented of the c(10) ring from Saccharomyces cerevisiae determined at pH 8.3, 6.1 and 5.5, at resolutions of 2.0 Å, 2.5 Å and 2.0 Å, respectively. The overall structure of this mitochondrial c-ring is similar to known homologs, except that the essential carboxylate, Glu59, adopts an open extended conformation. Molecular dynamics simulations reveal that opening of the essential carboxylate is a consequence of the amphiphilic nature of the crystallization buffer. We propose that this new structure represents the functionally open form of the c subunit, which facilitates proton loading and release.