Structure of mycobacterial ATP synthase bound to the tuberculosis drug bedaquiline

H Guo, GM Courbon, SA Bueler, J Mai, J Liu… - Nature, 2021 - nature.com
Tuberculosis—the world's leading cause of death by infectious disease—is increasingly
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 …

[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 …

Structure of a bacterial ATP synthase

H Guo, T Suzuki, JL Rubinstein - Elife, 2019 - elifesciences.org
ATP synthases produce ATP from ADP and inorganic phosphate with energy from a
transmembrane proton motive force. Bacterial ATP synthases have been studied extensively …

The six steps of the complete F1-ATPase rotary catalytic cycle

M Sobti, H Ueno, H Noji, AG Stewart - Nature Communications, 2021 - nature.com
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 …

Cryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states

M Sobti, C Smits, ASW Wong, R Ishmukhametov… - Elife, 2016 - elifesciences.org
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 …

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 …

Changes within the central stalk of E. coli F1Fo ATP synthase observed after addition of ATP

M Sobti, YC Zeng, JL Walshe, SHJ Brown… - Communications …, 2023 - nature.com
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 …

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 …

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 …