Search results
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.
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.
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 · Nature Communications - F1Fo ATP synthase works using a rotary catalysis mechanism. Here, the authors report cryo-EM structures of Bacillus PS3 F1-ATPase encompassing the complete set of six...
21 cze 2019 · Cryo-EM single-particle analysis (table S1) of purified and active (fig. S1) Polytomella ATP synthase dimer yielded a map at 2.94 Å overall resolution. Local masking improved the resolution to 2.7 to 2.8 Å in overlapping regions covering the full complex (table S2 and figs. S2 and S3).
27 sie 2011 · Human mitochondrial (mt) ATP synthase, or complex V consists of two functional domains: F 1, situated in the mitochondrial matrix, and F o, located in the inner mitochondrial membrane. Complex V uses the energy created by the proton electrochemical gradient to phosphorylate ADP to ATP.
26 lis 1999 · Adenosine triphosphate (ATP) synthase contains a rotary motor involved in biological energy conversion. Its membrane-embedded F 0 sector has a rotation generator fueled by the proton-motive force, which provides the energy required for the synthesis of ATP by the F 1 domain.
