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

doi:10.1074/jbc.M117.778175

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Article

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

The Journal of biological chemistry - 12 May 2017

Călinescu Octavian, Dwivedi Manish, Patiño-Ruiz Miyer, Padan Etana, Fendler Klaus

Abstract excerpt

Na+/H+ antiporters are located in the cytoplasmic and intracellular membranes and play crucial roles in regulating intracellular pH, Na+, and volume. The NhaA antiporter of Escherichia coli is the best studied member of the Na+/H+ exchanger family and a model system for all related Na+/H+ exchangers, including eukaryotic representatives. Several amino acid residues are important for the transport activity of...

Read the complete abstract on PubMed

Topics

Biological Transport
Biological Transport, Active
Crystallography, X-Ray
Escherichia coli
Escherichia coli Proteins
Fluorometry

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Hydrogen-Ion Concentration

Lysine

Mutagenesis, Site-Directed

Mutation

Phenotype

Protein Structure, Secondary

Protein Transport

Sodium-Hydrogen Exchangers

Spectrometry, Fluorescence

Source

Open in PubMed Open full text

Identifiers

PMID: 28330875
DOI: 10.1074/jbc.M117.778175
PMCID: PMC5427271

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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