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1 wrz 2001 · ATP synthase is a ubiquitous, highly conserved enzyme that catalyses the formation of ATP from ADP and P i using a unique rotary motor mechanism. The enzyme is located in the inner membrane of...
3 sie 2021 · F1Fo ATP synthase interchanges phosphate transfer energy and proton motive force via a rotary catalysis mechanism.
5 wrz 2024 · We determined the structure of ATP synthase within mitochondria of the unicellular flagellate Polytomella by electron cryo-tomography and subtomogram averaging at up to 4.2-angstrom resolution, revealing six rotary positions of the central stalk, subclassified into 21 substates of the F 1 head.
The ATP synthase, also called Complex V, has two major subunits designated F 0 and F 1. The F 0 part, bound to inner mitochondrial membrane is involved in proton translocation, whereas the F 1 part found in the mitochondrial matrix is the water soluble catalytic domain.
Lai et al. determine the complete structures of human ATP synthase in three main rotational states and one substate, providing mechanistic insights into the structure and function of the ATP synthase complexes and laying a foundation for target-based drug discovery.
25 kwi 2022 · CryoEM of mitochondrial ATP synthase frozen during rotary catalysis reveals dramatic conformational changes in the peripheral stalk subcomplex, which enable the enzyme’s efficient synthesis of...
The ATP synthase in human mitochondria provides most cellular ATP under aerobic conditions. Energy derived from oxidative metabolism generates a proton-motive force (pmf) across the inner membrane of the organelle, and the ATP synthase harnesses the pmf to make ATP from ADP and phosphate (1, 2).Human ATP synthase is an assembly of 29 subunits of 18 types (including the regulatory protein IF 1 ...
