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"Mitochondrial ATP synthases form dimers, which assemble into long ribbons at the rims of the inner membrane cristae's rims. " We reconstituted detergent-purified mitochondrial ATP synthase dimers from the green algae Polytomella sp. Both species of ATP synthase dimers from both species self-assemble into rows and bend the lipid bilayer locally, according to Tomographic volumes. The dimer rows and the induced degree of membrane curvature closely resemble those found in the inner membrane cristae. Monomers of mitochondrial ATP synthase that have been reconstituted into liposomes are unable to stretch membranes and do not form rows. ".
Source link: https://www.osti.gov/biblio/1559185
"The proton-driven ATP synthase is made up of two rotary, stepping motors and an elastic power transmission. " F O's Pro Proton transportation by F O is firmly tied to the c-ring's rotation relative to other F O subunits. Ring rotation was restricted to rotation of the external helix within each hairpin-shaped c-subunit in the ring. The coupling between collective ring and individual subunit movements was independent of the ring's length, which differs among organisms. Ensembles of monomer and dimers extracted from complete c-rings demonstrated that the coupling between collective ring and individual subunit motions was demonstrated. Both ring rotary and bending motions are shown by the correlation with key collective movements. Noncontact couplings between IB-GGGG motifs matched both the coevolution signal and contact couplings, as well as contact couplings. The residue coevolution reveals the physiological significance of the system that can link proton transfer to ring compliance, which can be traced back to ring compliance. ".
Source link: https://www.osti.gov/biblio/1213689
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