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TitleCryo-EM structure of Chlamydomonas reinhardtii chloroplast FF-ATP synthase.
Journal, issue, pagesBiochem Biophys Res Commun, Vol. 811, Page 153552, Year 2026
Publish dateApr 30, 2026
AuthorsJian Liu / Danyang Li / Qiang Wang / Ping Yin / Zeyuan Guan / Junjie Yan /
PubMed AbstractFF-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 ...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.
External linksBiochem Biophys Res Commun / PubMed:41819751
MethodsEM (single particle)
Resolution3.2 Å
Structure data

68717

22vl

EMDB-68717, PDB-22vl:
Cryo-EM structure of Chlamydomonas reinhardtii chloroplast F1Fo-ATP synthase
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

Source
  • chlamydomonas reinhardtii (plant)
KeywordsELECTRON TRANSPORT / Chlamydomonas reinhardtii / chloroplast / F1Fo-ATP synthase

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