English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Ligand-induced conformational dynamics of the Escherichia coli Na+/H+ antiporter NhaA revealed by hydrogen/deuterium exchange mass spectrometry

Eisinger, M. L., Dörrbaum, A. R., Michel, H., Padan, E., & Langer, J. D. (2017). Ligand-induced conformational dynamics of the Escherichia coli Na+/H+ antiporter NhaA revealed by hydrogen/deuterium exchange mass spectrometry. Proceedings of the National Academy of Sciences of the United States of America, 114(44), 11691-11696. doi:10.1073/pnas.1703422114.

Item is

Basic

show hide
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Eisinger, Martin L.1, Author           
Dörrbaum, Aline Ricarda1, 2, Author           
Michel, Hartmut1, Author           
Padan, Etana3, Author
Langer, Julian David1, 2, Author           
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society, ou_2461710              
3Silberman Institute of Life Sciences, Hebrew University, Jerusalem 91904, Israel, ou_persistent22              

Content

show
hide
Free keywords: NhaA; HDX-MS; conformational change; antiporter; membrane protein
 Abstract: Na+/H+ antiporters comprise a family of membrane proteins evolutionarily conserved in all kingdoms of life and play an essential role in cellular ion homeostasis. The NhaA crystal structure of Escherichia coli has become the paradigm for this class of secondary active transporters. However, structural data are only available at low pH, where NhaA is inactive. Here, we adapted hydrogen/deuterium-exchange mass spectrometry (HDX-MS) to analyze conformational changes in NhaA upon Li+ binding at physiological pH. Our analysis revealed a global conformational change in NhaA with two sets of movements around an immobile binding site. Based on these results, we propose a model for the ion translocation mechanism that explains previously controversial data for this antiporter. Furthermore, these findings contribute to our understanding of related human transporters that have been linked to various diseases.

Details

show
hide
Language(s): eng - English
 Dates: 2017-10-312017-10-31
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1073/pnas.1703422114
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : Proceedings of the National Academy of Sciences of the USA
  Other : Proc. Acad. Sci. USA
  Other : Proc. Acad. Sci. U.S.A.
  Abbreviation : PNAS
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 114 (44) Sequence Number: - Start / End Page: 11691 - 11696 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230