Sandbox Reserved 819: Difference between revisions
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The trimeric structure functions as a light-driven proton pump thanks to a retinal molecule, called <scene name='56/568017/New_scene_ret_2/1'>RET</scene>, which changes its conformation when absorbing a photon, resulting in a conformational change of the surrounding protein and the proton pumping action. Others ligands are linked with each subunit of the trimeric structure like the bacterioruberin (<scene name='56/568017/22b/1'>22B</scene>). | The trimeric structure functions as a light-driven proton pump thanks to a retinal molecule, called <scene name='56/568017/New_scene_ret_2/1'>RET</scene>, which changes its conformation when absorbing a photon, resulting in a conformational change of the surrounding protein and the proton pumping action. Others ligands are linked with each subunit of the trimeric structure like the bacterioruberin (<scene name='56/568017/22b/1'>22B</scene>). THe bacterioruberin plays a structural role for the trimerization of aR2. Several saccharides are also linked to the trimeric structure. | ||
Some lipids and glycolipids interact with the trimeric structure like the 2,3-di-phytanyl-glycerol (<scene name='56/568017/New_scene_3/1'>L2P</scene>) . They fill the intratrimer hydrophobic space and they are required to the complex activity. Others lipids surround the trimeric structure, which is essential to preserve it.<ref>PMID:18082767</ref> | Some lipids and glycolipids interact with the trimeric structure like the 2,3-di-phytanyl-glycerol (<scene name='56/568017/New_scene_3/1'>L2P</scene>) . They fill the intratrimer hydrophobic space and they are required to the complex activity. Others lipids surround the trimeric structure, which is essential to preserve it.<ref>PMID:18082767</ref> | ||