scholarly journals Analyzing conformational changes in single FRET-labeled A1 parts of archaeal A1AO-ATP synthase

2018 ◽  
Author(s):  
Gerhard Grüber ◽  
Michael Börsch ◽  
Hendrik Sielaff ◽  
Dhirendra Singh
Keyword(s):  
Atp Synthase ◽  
Conformational Changes ◽  
A1ao Atp Synthase

Isolation of a complete A1AO ATP synthase comprising nine subunits from the hyperthermophile Methanococcus jannaschii

Extremophiles ◽  
2003 ◽  
Vol 7 (3) ◽  
pp. 249-257 ◽  
Author(s):  
Astrid Lingl ◽  
Harald Huber ◽  
Karl O. Stetter ◽  
Frank Mayer ◽  
Josef Kellermann ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Methanococcus Jannaschii ◽  
A1ao Atp Synthase

A second transient position of ATP on its trail to the nucleotide-binding site of subunit B of the motor protein A1AO ATP synthase

2009 ◽  
Vol 166 (1) ◽  
pp. 38-45 ◽  
Author(s):  
Malathy Sony Subramanian Manimekalai ◽  
Anil Kumar ◽  
Asha Manikkoth Balakrishna ◽  
Gerhard Grüber
Keyword(s):  
Binding Site ◽  
Atp Synthase ◽  
Motor Protein ◽  
Nucleotide Binding ◽  
Nucleotide Binding Site ◽  
A1ao Atp Synthase ◽  
Subunit B

scholarly journals Structure of mycobacterial ATP synthase with the TB drug bedaquiline

2020 ◽  
Author(s):  
Hui Guo ◽  
Gautier M. Courbon ◽  
Stephanie A. Bueler ◽  
Juntao Mai ◽  
Jun Liu ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Conformational Changes ◽  
Atp Hydrolysis ◽  
Tight Binding ◽  
Multidrug Resistant ◽  
Energy Conditions ◽  
Binding Pockets ◽  
Obligate Aerobic ◽  
Essential Enzyme ◽  
Drug Free

SummaryTuberculosis (TB), the leading cause of death by infectious disease worldwide, is increasingly resistant to first line antibiotics. Developed from a screen against Mycobacterium smegmatis, bedaquiline can sterilize even latent M. tuberculosis infections that may otherwise persist for decades and has become a cornerstone of treatment for multidrug resistant and extensively-drug resistant TB. Bedaquiline targets mycobacterial ATP synthase, an essential enzyme in the obligate aerobic Mycobacterium genus. However, how the drug binds the intact enzyme is unknown. We determined the structure of M. smegmatis ATP synthase with and without bedaquiline. The drug-free structure reveals hook-like extensions from the enzyme’s α subunits that inhibit ATP hydrolysis in low-energy conditions, such as during latent infections. Bedaquiline binding induces global conformational changes in ATP synthase, creating tight binding pockets at the interface of subunits a and c. These binding sites explain the drug’s structure-activity relationship and its potency as an antibiotic for TB.

scholarly journals Large conformational changes of the   subunit in the bacterial F1F0 ATP synthase provide a ratchet action to regulate this rotary motor enzyme

2001 ◽  
Vol 98 (12) ◽  
pp. 6560-6564 ◽  
Author(s):  
S. P. Tsunoda ◽  
A. J. W. Rodgers ◽  
R. Aggeler ◽  
M. C. J. Wilce ◽  
M. Yoshida ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Conformational Changes ◽  
F1f0 Atp Synthase ◽  
Rotary Motor

A sodium ion-dependent A1AO ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus

FEBS Journal ◽  
2007 ◽  
Vol 274 (15) ◽  
pp. 3928-3938 ◽  
Author(s):  
Kim Y. Pisa ◽  
Harald Huber ◽  
Michael Thomm ◽  
Volker Müller
Keyword(s):  
Atp Synthase ◽  
Pyrococcus Furiosus ◽  
Sodium Ion ◽  
Hyperthermophilic Archaeon ◽  
A1ao Atp Synthase

scholarly journals Binding of subunit E into the A–B interface of the A1AO ATP synthase

2011 ◽  
Vol 1808 (9) ◽  
pp. 2111-2118 ◽  
Author(s):  
Cornelia Hunke ◽  
Martin Antosch ◽  
Volker Müller ◽  
Gerhard Grüber
Keyword(s):  
Atp Synthase ◽  
A1ao Atp Synthase ◽  
Subunit E
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