9W2T
Cryo-EM structure of Fo domain of FoF1-ATPase monomer state on the bovine heart submitochondrial particles
Summary for 9W2T
| Entry DOI | 10.2210/pdb9w2t/pdb |
| EMDB information | 65579 |
| Descriptor | ATP synthase F(0) complex subunit 8, ATP synthase F(0) complex subunit k, mitochondrial, ATP synthase F(0) complex subunit C1, mitochondrial, ... (10 entities in total) |
| Functional Keywords | atp synthase, fof1-atpase, submitochondrial particles, motor protein |
| Biological source | Bos taurus (domestic cattle) More |
| Total number of polymer chains | 17 |
| Total formula weight | 146180.52 |
| Authors | Nakano, A.,Masuya, T.,Akisada, S.,Ishikawa-Fukuda, M.,Mitsuoka, K.,Miyoshi, H.,Murai, M.,Yokoyama, K. (deposition date: 2025-07-28, release date: 2026-04-01) |
| Primary citation | Nakano, A.,Masuya, T.,Akisada, S.,Ishikawa-Fukuda, M.,Mitsuoka, K.,Miyoshi, H.,Murai, M.,Yokoyama, K. Structures of respiratory supercomplexes and ATP synthase oligomers in mammalian mitochondrial inner membrane. Nat Commun, 2026 Cited by PubMed Abstract: Understanding the functional mechanisms of membrane protein complexes requires structural analysis within their native membrane environment. Here, we applied cryo-electron microscopy to determine the structures of FF ATP synthase and respiratory supercomplexes (SCs) on sub-mitochondrial particles (SMPs) isolated from bovine heart mitochondria. Most FF complexes were observed as dimers stabilized by the regulatory factor IF₁, and a tetrameric assembly comprising two FF-IF₁ dimers arranged linearly was also identified. This finding indicates that the tetrameric units of FF are present in the mitochondrial inner membrane and contribute to shaping cristae tips in mammalian mitochondria. F domain maps resolve the e-subunit- c₈-ring interface and show no discrete density for a tightly bound lipid within the c₈-ring. In addition to the previously reported SCs compositions CI₁CIII₂CIV₁ and CI₁CIII₂CIV₂, our analysis identified an additional assembly with the composition CI₁CIII₂CIV₃, as well as a CI₂CIII₂CIV₆ mega-complex. This approach enables rapid structural determination of FF ATP synthase and SCs from minimal membrane fractions, providing a foundation for elucidating the molecular basis of metabolic disorders and mitochondrial diseases at the level of higher-order architecture. PubMed: 41844608DOI: 10.1038/s41467-026-70578-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.1 Å) |
Structure validation
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