3U32
ATP synthase c10 ring reacted with DCCD at pH 5.5
Summary for 3U32
| Entry DOI | 10.2210/pdb3u32/pdb |
| Related | 2WGM 2X2V 2XOK 2XQU 3U2F 3U2Y |
| Descriptor | ATP synthase subunit C, mitochondrial, DICYCLOHEXYLUREA (3 entities in total) |
| Functional Keywords | f1fo atp synthase, proton pore, c10 ring, dccd-reacted, 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 | 40073.64 |
| Authors | Symersky, J.,Pagadala, V.,Osowski, D.,Krah, A.,Meier, T.,Faraldo-Gomez, J.,Mueller, D.M. (deposition date: 2011-10-04, release date: 2012-02-08, Last modification date: 2024-11-20) |
| 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 Cited by 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: 22504883DOI: 10.1038/nsmb.2284 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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