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Article

Beta-sheet-dependent dimerization is essential for the stability of NhaA Na+/H+ antiporter.

The Journal of biological chemistry - 6 Mar 2009

Herz Katia, Rimon Abraham, Jeschke Gunnar, Padan Etana

Abstract excerpt

A structural model of the NhaA dimer showed that a beta-hairpin of each monomer combines to form a beta-sheet at the periplasmic side of the membrane. By Cys scanning the entire beta-hairpin and testing each Cys replacement for functionality and intermolecular cross-linking, we found that Gln47 a...

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Source

Identifiers

PMID: 19129192
DOI: 10.1074/jbc.M807720200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19129192-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

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Beta-sheet-dependent dimerization is essential for the stability of NhaA Na+/H+ antiporter.PMID 19129192Read ↗

NhaA antiporter functions using 10 helices, and an additional 2 contribute to assembly/stability.Semantic proximity Read ↗

Helix VIII of NhaA Na(+)/H(+) antiporter participates in the periplasmic cation passage and pH regulation of the antiporter.Semantic proximity Read ↗

Transmembrane segment II of NhaA Na+/H+ antiporter lines the cation passage, and Asp65 is critical for pH activation of the antiporter.Semantic proximity Read ↗

Oligomerization of NhaA, the Na+/H+ antiporter of Escherichia coli in the membrane and its functional and structural consequences.Semantic proximity Read ↗

Lysine 300 is essential for stability but not for electrogenic transport of the Escherichia coli NhaA Na+/H+ antiporter.Semantic proximity Read ↗

Revealing the ligand binding site of NhaA Na+/H+ antiporter and its pH dependence.Semantic proximity Read ↗

Mutation E252C increases drastically the Km value for Na+ and causes an alkaline shift of the pH dependence of NhaA Na+/H+ antiporter of Escherichia coli.Semantic proximity Read ↗

Trans membrane domain IV is involved in ion transport activity and pH regulation of the NhaA-Na(+)/H(+) antiporter of Escherichia coli.Semantic proximity Read ↗

Regulation of NhaA by protons.Semantic proximity Read ↗

Site-directed mutations reflecting functional and structural properties of Ec-NhaA.Semantic proximity Read ↗

A pH-dependent conformational change of NhaA Na(+)/H(+) antiporter of Escherichia coli involves loop VIII-IX, plays a role in the pH response of the protein, and is maintained by the pure protein in dodecyl maltoside.Semantic proximity Read ↗

NhaA of Escherichia coli, as a model of a pH-regulated Na+/H+antiporter.Semantic proximity Read ↗

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