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Mitochondrial ATP synthase is mostly isolated in monomeric form, but in the inner mitochondrial membrane it seems to dimerize and to form higher oligomeric structures from dimeric building blocks. Following a period of electron microscopic single particle analyses that revealed an angular orientation of the membrane parts of monomeric ATP synthases in the dimeric structures, and after extensive studies...
Specific modules and subcomplexes like F 1 and F 0 -parts, F 1 -c subcomplexes, peripheral and central stalks, and the rotor part comprising a ring of c-subunits with attached subunits γ, δ, and ε can be identified in yeast and mammalian ATP synthase. Four subunits, α 3 β 3 , OSCP, and h, seem to form a structural entity at the extramembranous rotor/stator interface...
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