Structure of mycobacterial ATP synthase bound to the tuberculosis drug bedaquiline
Tuberculosis—the world's leading cause of death by infectious disease—is increasingly
resistant to current first-line antibiotics. The bacterium Mycobacterium tuberculosis (which …
resistant to current first-line antibiotics. The bacterium Mycobacterium tuberculosis (which …
Cryo-EM of ATP synthases
H Guo, JL Rubinstein - Current Opinion in Structural Biology, 2018 - Elsevier
Highlights•Cryo-EM structures of mitochondrial and bacterial ATP synthases have been
determined between∼ 7 and∼ 3.6 Å resolution.•Purified ATP synthase complexes exist in …
determined between∼ 7 and∼ 3.6 Å resolution.•Purified ATP synthase complexes exist in …
[HTML][HTML] ATP synthase from Escherichia coli: Mechanism of rotational catalysis, and inhibition with the ε subunit and phytopolyphenols
M Nakanishi-Matsui, M Sekiya, M Futai - Biochimica et Biophysica Acta …, 2016 - Elsevier
Abstract ATP synthases (F o F 1) are found ubiquitously in energy-transducing membranes
of bacteria, mitochondria, and chloroplasts. These enzymes couple proton transport and …
of bacteria, mitochondria, and chloroplasts. These enzymes couple proton transport and …
Structure of a bacterial ATP synthase
ATP synthases produce ATP from ADP and inorganic phosphate with energy from a
transmembrane proton motive force. Bacterial ATP synthases have been studied extensively …
transmembrane proton motive force. Bacterial ATP synthases have been studied extensively …
The six steps of the complete F1-ATPase rotary catalytic cycle
F1Fo ATP synthase interchanges phosphate transfer energy and proton motive force via a
rotary catalysis mechanism. Isolated F1-ATPase catalytic cores can hydrolyze ATP, passing …
rotary catalysis mechanism. Isolated F1-ATPase catalytic cores can hydrolyze ATP, passing …
Cryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states
A molecular model that provides a framework for interpreting the wealth of functional
information obtained on the E. coli F-ATP synthase has been generated using cryo-electron …
information obtained on the E. coli F-ATP synthase has been generated using cryo-electron …
Structure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 Å resolution
E Morales-Rios, MG Montgomery… - Proceedings of the …, 2015 - National Acad Sciences
The structure of the intact ATP synthase from the α-proteobacterium Paracoccus
denitrificans, inhibited by its natural regulatory ζ-protein, has been solved by X-ray …
denitrificans, inhibited by its natural regulatory ζ-protein, has been solved by X-ray …
Changes within the central stalk of E. coli F1Fo ATP synthase observed after addition of ATP
F1Fo ATP synthase functions as a biological generator and makes a major contribution to
cellular energy production. Proton flow generates rotation in the Fo motor that is transferred …
cellular energy production. Proton flow generates rotation in the Fo motor that is transferred …
Bedaquiline targets the ε subunit of mycobacterial F-ATP synthase
S Kundu, G Biukovic, G Grüber… - Antimicrobial agents and …, 2016 - Am Soc Microbiol
The tuberculosis drug bedaquiline inhibits mycobacterial F-ATP synthase by binding to its c
subunit. Using the purified ε subunit of the synthase and spectroscopy, we previously …
subunit. Using the purified ε subunit of the synthase and spectroscopy, we previously …
Beyond binding change: the molecular mechanism of ATP hydrolysis by F1-ATPase and its biochemical consequences
S Nath - Frontiers in Chemistry, 2023 - frontiersin.org
F1-ATPase is a universal multisubunit enzyme and the smallest-known motor that, fueled by
the process of ATP hydrolysis, rotates in 120o steps. A central question is how the …
the process of ATP hydrolysis, rotates in 120o steps. A central question is how the …