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ATP Synthase - Astrophysics Data System

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Last Updated: 10 June 2022

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Oligomycin frames a common drug-binding site in the ATP synthase

"We report the high-resolution crystal structure of oligomycin bound to the yeast mitochondrial ATP synthase's subunit c 10 ring. " Oligomycin binds to the surface of the c 10 ring, gaining in contact with two neighboring molecules in a way that explains the inhibitory action on ATP synthesis. The remaining contacts between oligomycin and subunit c are mainly hydrophobic. Human and yeast's amino acid residues are 100% preserved within the oligomycin-binding site, but they are quite different from those in bacterial homologs, leading to the disparate sensitivity to oligomycin.

Source link: https://ui.adsabs.harvard.edu/abs/2012PNAS..10913961S/abstract


Rate of hydrolysis in ATP synthase is fine-tuned by α-subunit motif controlling active site conformation

"F o F 1 ATP synthase is a model system: a small molecular machine synthesizing or hydrolyzing ATP using a rotary motor is an interesting model system: a complex molecular unit synthesizing or hydrolyzing ATP using a rotary motor. Hydrolysis is carried out by an Isolated F 1 at a rate that is highly sensitive to ATP concentrations. ATP is slowly hydrolyzed in the so-called tight binding site at low ATP levels, while at higher inclination levels, additional ATP molecules triggers rotation of the central u03b3-subunit, causing the site to switch from a loose binding site in which hydrolysis occurs faster. We explore how large macromolecular rearrangements may control the active site and how reaction rate changes with active site conformation by a combination of theoretical methods.

Source link: https://ui.adsabs.harvard.edu/abs/2013PNAS..110.2117B/abstract


Nonequilibrium fluctuations of lipid membranes by the rotating motor protein F 1 F 0 -ATP synthase

"The biological interaction of protein synthesis and bending elasticity is primarily determinative of membrane deformation's cellular capability. " When reconstituted in massive lipid vesicles, we find that ATP synthes the biochemical energy in cells by proton-pumping activity across the membrane, promotes localized nonequilibrium membrane fluctuations.

Source link: https://ui.adsabs.harvard.edu/abs/2017PNAS..11411291A/abstract

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions