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Journal Article
Integrating mass spectrometry with MD simulations reveals the role of lipids in Na+/H+ antiporters
2017
Overview
Na
+
/H
+
antiporters are found in all kingdoms of life and exhibit catalysis rates that are among the fastest of all known secondary-active transporters. Here we combine ion mobility mass spectrometry and molecular dynamics simulations to study the conformational stability and lipid-binding properties of the Na
+
/H
+
exchanger NapA from
Thermus thermophilus
and compare this to the prototypical antiporter NhaA from
Escherichia coli
and the human homologue NHA2. We find that NapA and NHA2, but not NhaA, form stable dimers and do not selectively retain membrane lipids. By comparing wild-type NapA with engineered variants, we show that the unfolding of the protein in the gas phase involves the disruption of inter-domain contacts. Lipids around the domain interface protect the native fold in the gas phase by mediating contacts between the mobile protein segments. We speculate that elevator-type antiporters such as NapA, and likely NHA2, use a subset of annular lipids as structural support to facilitate large-scale conformational changes within the membrane.
Na
+
/H
+
antiporters transport sodium or lithium ions across the membrane in exchange for protons. Here the authors combine ion mobility mass spectrometry and molecular dynamics simulations to uncover a facilitating role for lipids in the transport mechanism.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 82
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - metabolism
/ biokemi
/ Biologi med inriktning mot strukturbiologi
/ Biology with specialization in Structural Biology
/ E coli
/ Escherichia coli Proteins - chemistry
/ Escherichia coli Proteins - metabolism
/ Humanities and Social Sciences
/ Lipids
/ Molecular Dynamics Simulation
/ Proteins
/ Science
/ Sodium-Hydrogen Exchangers - chemistry
/ Sodium-Hydrogen Exchangers - genetics
