Deciphering the structural organization of the ternary protein complex that switches off photosynthesis
By their photosynthetic activity, microalgae are crucial actors in the CO2 pumping for the atmosphere. CO2 assimilation in photosynthetic organisms is performed in the Calvin cycle. A small chloroplastic protein, CP12 regulates two key enzymes of the Calvin cycle, glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and phosphoribulokinase (PRK) according to the circadian cycle and its redox state. CP12 contains 4 cysteine residues which form two disulfide bridges when CP12 is oxidized (which corresponds to the night conditions) and is partially disordered. CP12 then binds to GAPDH and PRK to form a ternary complex, thereby inhibiting the Calvin cycle. To decipher the molecular mechanisms of this inhibition, we need to solve the structural arrangement of this complex in solution. SANS with contrast variation is a method of choice for such an issue. SANS experiments on the ternary complex with hydrogenated and perdeuterated subunits of the complex will allow us to reveal the conformation and the respective position of each partner, and to follow in particular the conformational changes undergone by the intrinsically disordered protein CP12 upon complex formation.
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RECEVEUR BRECHOT; GABEL Frank; Launay Helene and MARTEL Anne. (2019). Deciphering the structural organization of the ternary protein complex that switches off photosynthesis. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-968
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