ArticleProceedings of the National Academy of Sciences of the United States of America2016
Regulation of the thermoalkaliphilic F1-ATPase from Caldalkalibacillus thermarum.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 53 citations in OpenAlex.
- Distinct structural features of Pseudomonas aeruginosa ATP synthase revealed by cryo-electron microscopy.Nature communications · 2025Article
- R103 and R115 Affinity Mutants of ATeam ATP Biosensors.Sensors (Basel, Switzerland) · 2025Article
- HFrontiers in microbiology · 2025Review
- The chloroplast ATP synthase redox domain inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- FInternational journal of molecular sciences · 2023Review
- Changes within the central stalk of E. coli FCommunications biology · 2023Article
- Rotary mechanism of V/A-ATPases-how is ATP hydrolysis converted into a mechanical step rotation in rotary ATPases?Frontiers in molecular biosciences · 2023Review
- ATP binding by an FFrontiers in molecular biosciences · 2023Article
- The six steps of the complete FNature communications · 2021Article
- Regulation of ATP hydrolysis by the ε subunit, ζ subunit and Mg-ADP in the ATP synthase of Paracoccus denitrificans.Biochimica et biophysica acta. Bioenergetics · 2021Article
- ATP-binding affinity of the ε subunit of thermophilic FBiochemistry and biophysics reports · 2020Article
- Disrupting coupling within mycobacterial F-ATP synthases subunit ε causes dysregulated energy production and cell wall biosynthesis.Scientific reports · 2019Article
- The N-terminal region of the ϵ subunit from cyanobacterial ATP synthase alone can inhibit ATPase activity.The Journal of biological chemistry · 2019Article
- Structure of FOpen biology · 2019Article
- Cryo-EM reveals distinct conformations ofeLife · 2019Article
- Turbine enzyme's structure in the crosshairs to target tuberculosis.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The structure of the catalytic domain of the ATP synthase fromProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Structure of a bacterial ATP synthase.eLife · 2019Article
- Control of rotation of the FJournal of bioenergetics and biomembranes · 2018Review
- The regulatory subunit ε in Escherichia coli FBiochimica et biophysica acta. Bioenergetics · 2018Review
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The crystal structure has been determined of the F1-catalytic domain of the F-ATPase from Caldalkalibacillus thermarum, which hydrolyzes adenosine triphosphate (ATP) poorly. It is very similar to those of active mitochondrial and bacterial F1-ATPases. In the F-ATPase from Geobacillus stearothermophilus, conformational changes in the ε-subunit are influenced by intracellular ATP concentration and membrane potential. When ATP is plentiful, the ε-subunit assumes a "down" state, with an ATP molecule bound to its two C-terminal α-helices; when ATP is scarce, the α-helices are proposed to inhibit ATP hydrolysis by assuming an "up" state, where the α-helices, devoid of ATP, enter the α3β3-catalytic region. However, in the Escherichia coli enzyme, there is no evidence that such ATP binding to the ε-subunit is mechanistically important for modulating the enzyme's hydrolytic activity. In the structure of the F1-ATPase from C. thermarum, ATP and a magnesium ion are bound to the α-helices in the down state. In a form with a mutated ε-subunit unable to bind ATP, the enzyme remains inactive and the ε-subunit is down. Therefore, neither the γ-subunit nor the regulatory ATP bound to the ε-subunit is involved in the inhibitory mechanism of this particular enzyme. The structure of the α3β3-catalytic domain is likewise closely similar to those of active F1-ATPases. However, although the βE-catalytic site is in the usual "open" conformation, it is occupied by the unique combination of an ADP molecule with no magnesium ion and a phosphate ion. These bound hydrolytic products are likely to be the basis of inhibition of ATP hydrolysis.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.