6FKH
Chloroplast F1Fo conformation 2
Summary for 6FKH
| Entry DOI | 10.2210/pdb6fkh/pdb |
| EMDB information | 4271 |
| Descriptor | ATP synthase subunit a, chloroplastic, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (12 entities in total) |
| Functional Keywords | atp synthase, membrane protein complex, molecular motor, membrane protein |
| Biological source | Spinacia oleracea (Spinach) More |
| Total number of polymer chains | 26 |
| Total formula weight | 597235.83 |
| Authors | Hahn, A.,Vonck, J.,Mills, D.J.,Meier, T.,Kuehlbrandt, W. (deposition date: 2018-01-24, release date: 2018-05-23, Last modification date: 2024-10-23) |
| Primary citation | Hahn, A.,Vonck, J.,Mills, D.J.,Meier, T.,Kuhlbrandt, W. Structure, mechanism, and regulation of the chloroplast ATP synthase. Science, 360:-, 2018 Cited by PubMed Abstract: The chloroplast adenosine triphosphate (ATP) synthase uses the electrochemical proton gradient generated by photosynthesis to produce ATP, the energy currency of all cells. Protons conducted through the membrane-embedded F motor drive ATP synthesis in the F head by rotary catalysis. We determined the high-resolution structure of the complete cFF complex by cryo-electron microscopy, resolving side chains of all 26 protein subunits, the five nucleotides in the F head, and the proton pathway to and from the rotor ring. The flexible peripheral stalk redistributes differences in torsional energy across three unequal steps in the rotation cycle. Plant ATP synthase is autoinhibited by a β-hairpin redox switch in subunit γ that blocks rotation in the dark. PubMed: 29748256DOI: 10.1126/science.aat4318 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.2 Å) |
Structure validation
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