22VL
Cryo-EM structure of Chlamydomonas reinhardtii chloroplast F1Fo-ATP synthase
Summary for 22VL
| Entry DOI | 10.2210/pdb22vl/pdb |
| EMDB information | 68717 |
| Descriptor | ATP synthase subunit a, chloroplastic, ATP synthase subunit beta, chloroplastic, MAGNESIUM ION, ... (12 entities in total) |
| Functional Keywords | chlamydomonas reinhardtii, chloroplast, f1fo-atp synthase, electron transport |
| Biological source | Chlamydomonas reinhardtii More |
| Total number of polymer chains | 26 |
| Total formula weight | 547336.71 |
| Authors | Liu, J.,Li, D.Y.,Guan, Z.Y.,Yin, P.,Yan, J.J. (deposition date: 2026-01-25, release date: 2026-06-17) |
| Primary citation | Liu, J.,Li, D.,Wang, Q.,Yin, P.,Guan, Z.,Yan, J. Cryo-EM structure of Chlamydomonas reinhardtii chloroplast F 1 F o -ATP synthase. Biochem.Biophys.Res.Commun., 811:153552-153552, 2026 Cited by PubMed Abstract: FF-ATP synthase is a multi-subunit energy-producing macromolecular machine, consisting of hydrophilic F and hydrophobic F segments, which utilize transmembrane electrochemical potential to synthesize ATP from ADP and inorganic phosphate. ATP synthases are widely distributed in the inner membrane of mitochondria, the thylakoid membrane of chloroplasts, and the plasma membrane of bacteria. To date, a comprehensively structural study on chloroplast FF-ATP synthase is very limited compared with their counterparts in mitochondria and bacteria. In this study, we in-situ extracted and purified chloroplast FF-ATP synthase from the photosynthetic unicellular green algae Chlamydomonas reinhardtii. The ATPase activity of the holoenzyme was validated by a combination of BN-PAGE separation and in-gel detection. We determined the structure of Chlamydomonas reinhardtii FF-ATP synthase at 3.2 Å resolution using single particle cryo-electron microscopy (cryo-EM). The structure is in an oxidized state with a disulfide bond formation in the γ subunit. More acidic residues were found to be involved in the proton translocation across the F segment compared with their counterparts of the higher plants. Overall, the structure presented here provides novel structural information, giving us comprehensive understanding of the photosynthetic chloroplast FF-ATP synthase from lower unicellular algae to higher plants. PubMed: 41819751DOI: 10.1016/j.bbrc.2026.153552 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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