ArticleScientific reports2016
The Ec-NhaA antiporter switches from antagonistic to synergistic antiport upon a single point mutation.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- The SLC-ome of membrane transport: from molecular discovery to physiology and clinical applications.Physiological reviews · 2026Review
- The evolution of a NaJournal of bacteriology · 2026Article
- pH-dependent activation of the NaNature communications · 2026Article
- The evolution of a NabioRxiv : the preprint server for biology · 2026Article
- Site-directed mutagenesis at the Glu78 in Ec-NhaA transporter impacting ion exchange: a biophysical study.European biophysics journal : EBJ · 2024Article
- The crossing of two unwound transmembrane regions that is the hallmark of the NhaA structural fold is critical for antiporter activity.Scientific reports · 2024Article
- Prokaryotic NaInternational journal of molecular sciences · 2022Review
- Insight into the direct interaction of NaScientific reports · 2021Article
- An angular motion of a conserved four-helix bundle facilitates alternating access transport in the TtNapA and EcNhaA transporters.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Cardiolipin is an Optimal Phospholipid for the Assembly, Stability, and Proper Functionality of the Dimeric Form of NhaA NaScientific reports · 2019Article
- Replacement of Lys-300 with a glutamine in the NhaA NaThe Journal of biological chemistry · 2019Article
- Ligand-induced conformational dynamics of theProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Lysine 300 is essential for stability but not for electrogenic transport of theThe Journal of biological chemistry · 2017Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Na(+), Li(+)/H(+) antiporter of Escherichia coli (Ec-NhaA) maintains pH, Na(+) homeostasis in enterobacteria. We used isothermal titration calorimetry to perform a detailed thermodynamic analysis of Li(+) binding to Ec-NhaA and several of its mutants. We found that, in line with the canonical alternative access mechanistic model of secondary transporters, Li(+)/H(+) binding to the antiporter is antagonistically coupled. Binding of Li(+) displaces 2 H(+) from the binding site. The process is enthalpically driven, the enthalpic gain just compensating for an entropic loss and the buffer-associated enthalpic changes dominate the overall free-energy change. Li(+) binding, H(+) release and antiporter activity were all affected to the same extent by mutations in the Li(+) binding site (D163E, D163N, D164N, D164E), while D133C changed the H(+)/Li(+) stoichiometry to 4. Most striking, however, was the mutation, A167P, which converted the Ec-NhaA antagonistic binding into synergistic binding which is only known to occur in Cl(-)/H(+) antiporter.
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