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Effects of lipid environment on the conformational changes of an ABC importer

In order to shuttle substrates across the lipid bilayer, membrane proteins undergo a series of conformation changes that are influenced by protein structure, ligands, and the lipid environment. To test the effect of lipid on conformation change of the ABC transporter MolBC, EPR studies were conducte...

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Autores principales: Rice, Austin J, Alvarez, Frances JD, Davidson, Amy L, Pinkett, Heather W
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4203734/
https://www.ncbi.nlm.nih.gov/pubmed/24852576
http://dx.doi.org/10.4161/chan.29294
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author Rice, Austin J
Alvarez, Frances JD
Davidson, Amy L
Pinkett, Heather W
author_facet Rice, Austin J
Alvarez, Frances JD
Davidson, Amy L
Pinkett, Heather W
author_sort Rice, Austin J
collection PubMed
description In order to shuttle substrates across the lipid bilayer, membrane proteins undergo a series of conformation changes that are influenced by protein structure, ligands, and the lipid environment. To test the effect of lipid on conformation change of the ABC transporter MolBC, EPR studies were conducted in lipids and detergents of variable composition. In both a detergent and lipid environment, MolBC underwent the same general conformation changes as detected by site-directed EPR spectroscopy. However, differences in activity and the details of the EPR analysis indicate conformational rigidity that is dependent on the lipid environment. From these observations, we conclude that native-like lipid mixtures provide the transporter with greater activity and conformational flexibility as well as technical advantages such as reconstitution efficiency and protein stability.
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spelling pubmed-42037342015-07-01 Effects of lipid environment on the conformational changes of an ABC importer Rice, Austin J Alvarez, Frances JD Davidson, Amy L Pinkett, Heather W Channels (Austin) Research Paper In order to shuttle substrates across the lipid bilayer, membrane proteins undergo a series of conformation changes that are influenced by protein structure, ligands, and the lipid environment. To test the effect of lipid on conformation change of the ABC transporter MolBC, EPR studies were conducted in lipids and detergents of variable composition. In both a detergent and lipid environment, MolBC underwent the same general conformation changes as detected by site-directed EPR spectroscopy. However, differences in activity and the details of the EPR analysis indicate conformational rigidity that is dependent on the lipid environment. From these observations, we conclude that native-like lipid mixtures provide the transporter with greater activity and conformational flexibility as well as technical advantages such as reconstitution efficiency and protein stability. Landes Bioscience 2014-07-01 2014-05-22 /pmc/articles/PMC4203734/ /pubmed/24852576 http://dx.doi.org/10.4161/chan.29294 Text en Copyright © 2014 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
spellingShingle Research Paper
Rice, Austin J
Alvarez, Frances JD
Davidson, Amy L
Pinkett, Heather W
Effects of lipid environment on the conformational changes of an ABC importer
title Effects of lipid environment on the conformational changes of an ABC importer
title_full Effects of lipid environment on the conformational changes of an ABC importer
title_fullStr Effects of lipid environment on the conformational changes of an ABC importer
title_full_unstemmed Effects of lipid environment on the conformational changes of an ABC importer
title_short Effects of lipid environment on the conformational changes of an ABC importer
title_sort effects of lipid environment on the conformational changes of an abc importer
topic Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4203734/
https://www.ncbi.nlm.nih.gov/pubmed/24852576
http://dx.doi.org/10.4161/chan.29294
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