Transmembrane Segment II of NhaA Na+/H+ Antiporter Lines the Cation Passage, and Asp65 Is Critical for pH Activation of the Antiporter

The crystal structure of Escherichia coli NhaA determined at pH 4 has provided insights into the mechanism of activity of a pH-regulated Na+/H+ antiporter. However, because NhaA is activated at physiological pH (pH 5.5–8.5), many questions related to the active state of NhaA have remained elusive. O...

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Veröffentlicht in:	The Journal of biological chemistry 2010-01, Vol.285 (3), p.2211-2220
Hauptverfasser:	Herz, Katia, Rimon, Abraham, Olkhova, Elena, Kozachkov, Lena, Padan, Etana
Format:	Artikel
Sprache:	eng
Schlagworte:	Aspartic Acid - metabolism Cations - metabolism Cell Membrane - drug effects Cell Membrane - metabolism Computer Simulation Conserved Sequence Crystal Structure-based Functional Study Crystallography, X-Ray Cysteine Escherichia coli - cytology Escherichia coli - genetics Escherichia coli - growth & development Escherichia coli - metabolism Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Gene Expression Regulation, Bacterial Hydrogen-Ion Concentration Ion Transport Lithium - metabolism Membrane Membrane Transport, Structure, Function, and Biogenesis Mesylates - pharmacology Models, Molecular Mutation Na+/H+ Antiporter NhaA NhaA pH-activation Periplasm - metabolism Phenotype Protein Conformation Sodium-Hydrogen Exchangers - chemistry Sodium-Hydrogen Exchangers - genetics Sodium-Hydrogen Exchangers - metabolism Transport Protein
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