|Title||Structure, mechanism, and regulation of the chloroplast ATP synthase.|
|Publication Type||Journal Article|
|Year of Publication||2018|
|Authors||Hahn, A, Vonck, J, Mills, DJ, Meier, T, Kühlbrandt, W|
|Date Published||2018 05 11|
|Keywords||Adenosine Triphosphate, Chloroplast Proton-Translocating ATPases, Chloroplasts, Cryoelectron Microscopy, Evolution, Molecular, Molecular Motor Proteins, Plant Leaves, Protein Conformation, Protein Subunits, Rotation, Spinacia oleracea|
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.
|Grant List||/ / Wellcome Trust / United Kingdom|