ArticleThe Journal of biological chemistry2012
Revealing the ligand binding site of NhaA Na+/H+ antiporter and its pH dependence.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 57 citations in OpenAlex.
- pH-dependent activation of the NaNature communications · 2026Article
- Structure and mechanism of the KNature communications · 2024Article
- 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
- Article
- Thermodynamically consistent determination of free energies and rates in kinetic cycle models.Biophysical reports · 2023Article
- Thermodynamically consistent determination of free energies and rates in kinetic cycle models.bioRxiv : the preprint server for biology · 2023Article
- Structure-Guided Identification of Critical Residues in the Vacuolar Cation/Proton Antiporter NHX1 fromPlants (Basel, Switzerland) · 2023Article
- Crystal structure of the NaNature communications · 2022Article
- Prokaryotic NaInternational journal of molecular sciences · 2022Review
- Insight into the direct interaction of NaScientific reports · 2021Article
- Structure and elevator mechanism of the mammalian sodium/proton exchanger NHE9.The EMBO journal · 2020Article
- Alternative proton-binding site and long-distance coupling inProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Diverse Physiological Functions of Cation Proton Antiporters across Bacteria and Plant Cells.International journal of molecular sciences · 2020Review
- Replacement of Lys-300 with a glutamine in the NhaA NaThe Journal of biological chemistry · 2019Article
- Characterisation of sensor kinase by CD spectroscopy: golden rules and tips.Biochemical Society transactions · 2018Review
- Broad phylogenetic analysis of cation/proton antiporters reveals transport determinants.Nature communications · 2018Article
- Critical Functions of Region 1-67 and Helix XIII in Retaining the Active Structure of NhaD Antiporter inFrontiers in microbiology · 2018Article
- 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
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
pH and Na(+) homeostasis in all cells requires Na(+)/H(+) antiporters. In most cases, their activity is tightly pH-regulated. NhaA, the main antiporter of Escherichia coli, has homologues in all biological kingdoms. The crystal structure of NhaA provided insights into the mechanism of action and pH regulation of an antiporter. However, the active site of NhaA remained elusive because neither Na(+) nor Li(+), the NhaA ligands, were observed in the structure. Using isothermal titration calorimetry, we show that purified NhaA binds Li(+) in detergent micelles. This interaction is driven by an increase in enthalpy (ΔH of -8000 ± 300 cal/mol and ΔS of -15.2 cal/mol/degree at 283 K), involves a single binding site per NhaA molecule, and is highly specific and drastically dependent on pH; Li(+) binding was observed only at pH 8.5. Combining mutational analysis with the isothermal titration calorimetry measurements revealed that Asp-163, Asp-164, Thr-132, and Asp-133 form the Li(+) binding site, whereas Lys-300 plays an important role in pH regulation of the antiporter.
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Registered trials
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.