Site-directed tryptophan fluorescence reveals two essential conformational changes in the Na+/H+ antiporter NhaA. (Q35229161)

7 August 2017

title

Site-directed tryptophan fluorescence reveals two essential conformational changes in the Na+/H+ antiporter NhaA. (English)

1 reference

7 August 2017

Lena Kozachkov

1

1 reference

7 August 2017

Etana Padan

series ordinal

2

1 reference

7 August 2017

language of work or name

English

0 references

publication date

23 August 2011

1 reference

Proceedings of the National Academy of Sciences of the United States of America

7 August 2017

published in

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7 August 2017

volume

108

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7 August 2017

issue

38

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7 August 2017

page(s)

15769-15774

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Transport mechanism and pH regulation of the Na+/H+ antiporter NhaA from Escherichia coli: an electrophysiological study

7 August 2017

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

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Structure-based functional study reveals multiple roles of transmembrane segment IX and loop VIII-IX in NhaA Na+/H+ antiporter of Escherichia coli at physiological pH

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27 July 2018

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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+.

21 January 2018

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Unraveling functional and structural interactions between transmembrane domains IV and XI of NhaA Na+/H+ antiporter of Escherichia coli

21 January 2018

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Combined computational and biochemical study reveals the importance of electrostatic interactions between the "pH sensor" and the cation binding site of the sodium/proton antiporter NhaA of Escherichia coli.

21 January 2018

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Mutation E252C Increases Drastically the K Value for Na+ and Causes an Alkaline Shift of the pH Dependence of NhaA Na+/H+ Antiporter of Escherichia coli

21 January 2018

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

21 January 2018

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Ion extrusion systems in Escherichia coli

21 January 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/21873214

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Overproduction and purification of a functional Na+/H+ antiporter coded by nhaA (ant) from Escherichia coli

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/21873214

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Histidine 225, a residue of the NhaA-Na+/H+ antiporter of Escherichia coli is exposed and faces the cell exterior

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/21873214

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1073/PNAS.1109256108

1 reference

7 August 2017

0 references

1 reference

7 August 2017

1 reference