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Article

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

Proceedings of the National Academy of Sciences of the United States of America - 13 Oct 2015

Padan Etana, Danieli Tsafi, Keren Yael, Alkoby Dudu, Masrati Gal, Haliloglu Turkan, Ben-Tal Nir, Rimon Abraham

Abstract excerpt

The Escherichia coli Na(+)/H(+) antiporter (Ec-NhaA) is the best-characterized of all pH-regulated Na(+)/H(+) exchangers that control cellular Na(+) and H(+) homeostasis. Ec-NhaA has 12 helices, 2 of which (VI and VII) are absent from other antiporters that share the Ec-NhaA structural fold. This α-hairpin is located in the dimer interface of the Ec-NhaA homodimer together with a β-sheet. Here we examine...

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Share to Escherichia coli Proteins
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 26417087
DOI: 10.1073/pnas.1510964112
PMCID: PMC4611637

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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