3U2F

ATP synthase c10 ring in proton-unlocked conformation at PH 8.3

Summary for 3U2F

• Entry DOI: 10.2210/pdb3u2f/pdb
• Related: 2WGM 2X2V 2XOK 2XQU 3U2Y 3U32
• Descriptor: ATP synthase subunit C, mitochondrial (2 entities in total)
• Functional Keywords: f1fo atp synthase, proton pore, c10 ring, membrane protein
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Mitochondrion membrane; Multi-pass membrane protein (Potential): P61829
• Total number of polymer chains: 5
• Total formula weight: 38951.93

Authors

Symersky, J.,Pagadala, V.,Osowski, D.,Krah, A.,Meier, T.,Faraldo-Gomez, J.,Mueller, D.M. (deposition date: 2011-10-03, release date: 2012-02-08, Last modification date: 2023-09-13)

Primary citation

Symersky, J.,Pagadala, V.,Osowski, D.,Krah, A.,Meier, T.,Faraldo-Gomez, J.D.,Mueller, D.M.
Structure of the c(10) ring of the yeast mitochondrial ATP synthase in the open conformation.
Nat.Struct.Mol.Biol., 19:485-491, 2012

PubMed 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.

PubMed: 22504883
DOI: 10.1038/nsmb.2284

Experimental method

X-RAY DIFFRACTION (2 Å)