ArticlePLoS biology2013
A new type of Na(+)-driven ATP synthase membrane rotor with a two-carboxylate ion-coupling motif.
Article in PLoS biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Uncovering hidden phylo- and ecogenomic diversity of the widespread methanotrophic genus Methylobacter.FEMS microbiology ecology · 2026Article
- Structural and mechanistic basis of the central energy-converting methyltransferase complex of methanogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- ATP yield of plant respiration: potential, actual and unknown.Annals of botany · 2023Article
- Directed proton transfer from FBiophysical reviews · 2023Review
- NaNature chemical biology · 2022Article
- Genomic and Functional Variation of the ChlorophyllMicroorganisms · 2022Article
- Preliminary functional analysis of the subgingival microbiota of cats with periodontitis and feline chronic gingivostomatitis.Scientific reports · 2021Article
- ATP synthase: Evolution, energetics, and membrane interactions.The Journal of general physiology · 2020Review
- Unusual features of the c-ring of FScientific reports · 2019Article
- Why Nature Chose Potassium.Journal of molecular evolution · 2019Review
- Structure of FOpen biology · 2019Article
- Inward-facing conformation of a multidrug resistance MATE family transporter.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Broadly conserved NaProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Shewanella oneidensis MR-1 Utilizes both Sodium- and Proton-Pumping NADH Dehydrogenases during Aerobic Growth.Applied and environmental microbiology · 2018Article
- Insights into the regulatory function of theOpen biology · 2018Review
- Metabolism and Occurrence of Methanogenic and Sulfate-Reducing Syntrophic Acetate Oxidizing Communities in Haloalkaline Environments.Frontiers in microbiology · 2018Article
- Predicted Structures of the Proton-Bound Membrane-Embedded Rotor Rings of the Saccharomyces cerevisiae and Escherichia coli ATP Synthases.The journal of physical chemistry. B · 2017Article
- Molecular architecture of the N-type ATPase rotor ring fromEMBO reports · 2017Article
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9 authors.
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Abstract
The anaerobic bacterium Fusobacterium nucleatum uses glutamate decarboxylation to generate a transmembrane gradient of Na⁺. Here, we demonstrate that this ion-motive force is directly coupled to ATP synthesis, via an F₁F₀-ATP synthase with a novel Na⁺ recognition motif, shared by other human pathogens. Molecular modeling and free-energy simulations of the rotary element of the enzyme, the c-ring, indicate Na⁺ specificity in physiological settings. Consistently, activity measurements showed Na⁺ stimulation of the enzyme, either membrane-embedded or isolated, and ATP synthesis was sensitive to the Na⁺ ionophore monensin. Furthermore, Na⁺ has a protective effect against inhibitors targeting the ion-binding sites, both in the complete ATP synthase and the isolated c-ring. Definitive evidence of Na⁺ coupling is provided by two identical crystal structures of the c₁₁ ring, solved by X-ray crystallography at 2.2 and 2.6 Å resolution, at pH 5.3 and 8.7, respectively. Na⁺ ions occupy all binding sites, each coordinated by four amino acids and a water molecule. Intriguingly, two carboxylates instead of one mediate ion binding. Simulations and experiments demonstrate that this motif implies that a proton is concurrently bound to all sites, although Na⁺ alone drives the rotary mechanism. The structure thus reveals a new mode of ion coupling in ATP synthases and provides a basis for drug-design efforts against this opportunistic pathogen.
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