| Site-directed mutagenesis at the Glu78 in Ec-NhaA transporter impacting ion exchange: a biophysical study. | Site-directed mutagenesis at the Glu78 in Ec-NhaA transporter impacting ion exchange: a biophysical study.
Yadav A, Kumar D, Dwivedi M. | 07/16/2024 |
| Towards Molecular Understanding of the pH Dependence Characterizing NhaA of Which Structural Fold is Shared by Other Transporters. | Towards Molecular Understanding of the pH Dependence Characterizing NhaA of Which Structural Fold is Shared by Other Transporters.
Mondal R, Rimon A, Masrati G, Ben-Tal N, Friedler A, Padan E. | 11/6/2021 |
| An angular motion of a conserved four-helix bundle facilitates alternating access transport in the TtNapA and EcNhaA transporters. | An angular motion of a conserved four-helix bundle facilitates alternating access transport in the TtNapA and EcNhaA transporters.
Masrati G, Mondal R, Rimon A, Kessel A, Padan E, Lindahl E, Ben-Tal N., Free PMC Article | 02/6/2021 |
| Alternative proton-binding site and long-distance coupling in Escherichia coli sodium-proton antiporter NhaA. | Alternative proton-binding site and long-distance coupling in Escherichia coli sodium-proton antiporter NhaA.
Henderson JA, Huang Y, Beckstein O, Shen J., Free PMC Article | 12/5/2020 |
| findings indicate that alternative mechanisms sustain EcNhaA activity in the absence of canonical ion-binding residues and that the conserved lysines confer structural stability. | Replacement of Lys-300 with a glutamine in the NhaA Na(+)/H(+) antiporter of Escherichia coli yields a functional electrogenic transporter.
Patiño-Ruiz M, Dwivedi M, Călinescu O, Karabel M, Padan E, Fendler K., Free PMC Article | 04/13/2019 |
| analysis of NhaA pH-dependent activation by molecular dynamics simulation of atomic details of proton-coupled transport across membrane | Mechanism of pH-dependent activation of the sodium-proton antiporter NhaA.
Huang Y, Chen W, Dotson DL, Beckstein O, Shen J., Free PMC Article | 09/29/2018 |
| Lysine 300 has an essential role in stability but not electrogenic transport of Escherichia coli NhaA | Lysine 300 is essential for stability but not for electrogenic transport of the Escherichia coli NhaA Na(+)/H(+) antiporter.
Călinescu O, Dwivedi M, Patiño-Ruiz M, Padan E, Fendler K., Free PMC Article | 07/15/2017 |
| Data show that the Li(+) binding, H(+) release and antiporter activity were all affected to the same extent by Na(+), Li(+)/H(+) antiporter (NhaA) mutations in the Li(+) binding site (D163E, D163N, D164N, D164E). | The Ec-NhaA antiporter switches from antagonistic to synergistic antiport upon a single point mutation.
Dwivedi M, Sukenik S, Friedler A, Padan E., Free PMC Article | 02/4/2017 |
| Data show that the two aspartic acid residues of Na+/H+ antiporter NhaA, D163 and D164, act as Na+ trap and energetic barrier for the transport of Na+. | Simulating the function of sodium/proton antiporters.
Alhadeff R, Warshel A., Free PMC Article | 03/19/2016 |
| NhaA antiporter functions using 10 helices, and an additional 2 contribute to assembly/stability. | NhaA antiporter functions using 10 helices, and an additional 2 contribute to assembly/stability.
Padan E, Danieli T, Keren Y, Alkoby D, Masrati G, Haliloglu T, Ben-Tal N, Rimon A., Free PMC Article | 01/30/2016 |
| As it has been previously suggested that Asp163 is one of the two residues through which proton transport occurs, these results have clear implications to the current mechanistic models of sodium-proton antiport in NhaA. | Crystal structure of the sodium-proton antiporter NhaA dimer and new mechanistic insights.
Lee C, Yashiro S, Dotson DL, Uzdavinys P, Iwata S, Sansom MS, von Ballmoos C, Beckstein O, Drew D, Cameron AD., Free PMC Article | 07/25/2015 |
| Data indicate that mutating noninteracting residues to alanine have no effect on the pulling force of C-terminal transmembrane helices (TMHs) in membrane transport proteins CaiT, BtuC, NhaA, EmrD and GlpT. | Cotranslational folding of membrane proteins probed by arrest-peptide-mediated force measurements.
Cymer F, von Heijne G., Free PMC Article | 12/21/2013 |
| Data indicate that binding of Li+ to purified Na(+)/H(+) antiporter NhaA is enthalpy-driven, highly specific, and pH-dependent and involves a single binding site. | Revealing the ligand binding site of NhaA Na+/H+ antiporter and its pH dependence.
Maes M, Rimon A, Kozachkov-Magrisso L, Friedler A, Padan E., Free PMC Article | 01/26/2013 |
| Data show that a Trp at position 136 specifically monitors a pH-induced conformational change that activates NhaA, whereas a Trp at position 339 senses a ligand-induced conformational change that does not occur until NhaA is activated at alkaline pH. | Site-directed tryptophan fluorescence reveals two essential conformational changes in the Na+/H+ antiporter NhaA.
Kozachkov L, Padan E., Free PMC Article | 12/17/2011 |
| NhaA dimers are crucial for the stability of the antiporter under extreme stress conditions. | Beta-sheet-dependent dimerization is essential for the stability of NhaA Na+/H+ antiporter.
Herz K, Rimon A, Jeschke G, Padan E. | 01/21/2010 |
| A novel structural fold creates a delicately balanced electrostatic environment in the middle of the membrane, which might be essential for ion binding and translocation. Review. | The enlightening encounter between structure and function in the NhaA Na+-H+ antiporter.
Padan E. | 01/21/2010 |
| Model structure of the Na+/H+ exchanger 1 in human and E. coli | Model structure of the Na+/H+ exchanger 1 (NHE1): functional and clinical implications.
Landau M, Herz K, Padan E, Ben-Tal N. | 01/21/2010 |
| Na+/H+ antiporter genes may contribute to sodium-lithium countertransport activity and salt homeostasis in humans | A human Na+/H+ antiporter sharing evolutionary origins with bacterial NhaA may be a candidate gene for essential hypertension.
Xiang M, Feng M, Muend S, Rao R., Free PMC Article | 01/21/2010 |
| N-terminus verified by Edman degradation on complete protein | Histidine-226 is part of the pH sensor of NhaA, a Na+/H+ antiporter in Escherichia coli.
Gerchman Y, Olami Y, Rimon A, Taglicht D, Schuldiner S, Padan E., Free PMC Article | 11/5/2007 |
| under extreme stress conditions (0.1 m LiCl or 0.7 m NaCl at pH 8.5), the dimeric native NhaA was much more efficient than the monomeric mutant in conferring extreme stress resistance. | Monomers of the NhaA Na+/H+ antiporter of Escherichia coli are fully functional yet dimers are beneficial under extreme stress conditions at alkaline pH in the presence of Na+ or Li+.
Rimon A, Tzubery T, Padan E. | 01/21/2010 |
| combinatorial approach based on molecular dynamics simulations led to formulation of a model of NhaA transport mechanism, pH regulation & cation selectivity consistent with experimental data | Mechanism of Na+/H+ antiporting.
Arkin IT, Xu H, Jensen MØ, Arbely E, Bennett ER, Bowers KJ, Chow E, Dror RO, Eastwood MP, Flitman-Tene R, Gregersen BA, Klepeis JL, Kolossváry I, Shan Y, Shaw DE. | 01/21/2010 |
| folding rates of structural segments ranged from 0.31 s(-1) to 47 s(-1), providing detailed insight into a distinct folding hierarchy of an unfolded polypeptide into the native membrane protein structure | Observing folding pathways and kinetics of a single sodium-proton antiporter from Escherichia coli.
Kedrov A, Janovjak H, Ziegler C, Kuhlbrandt W, Muller DJ. | 01/21/2010 |
| The molecular interactions established on Na(+) binding may represent an early step in NhaA activation. | Locating ligand binding and activation of a single antiporter.
Kedrov A, Krieg M, Ziegler C, Kuhlbrandt W, Muller DJ., Free PMC Article | 01/21/2010 |
| functional and structural interactions between transmembrane domains; an active conformation of NhaA | Unraveling functional and structural interactions between transmembrane domains IV and XI of NhaA Na+/H+ antiporter of Escherichia coli.
Galili L, Herz K, Dym O, Padan E. | 01/21/2010 |
| In the passive downhill uptake mode pH regulation of the carrier affects both apparent Km as well as turnover (Vmax). | Kinetics of charge translocation in the passive downhill uptake mode of the Na+/H+ antiporter NhaA of Escherichia coli.
Zuber D, Krause R, Venturi M, Padan E, Bamberg E, Fendler K. | 01/21/2010 |