Martens, C, Stein, RA, Masureel, M et al. (7 more authors) (2016) Lipids modulate the conformational dynamics of a secondary multidrug transporter. Nature Structural & Molecular Biology, 23 (8). pp. 744-751. ISSN 1545-9993
Abstract
Direct interactions with lipids have emerged as key determinants of the folding, structure and function of membrane proteins, but an understanding of how lipids modulate protein dynamics is still lacking. Here, we systematically explored the effects of lipids on the conformational dynamics of the proton-powered multidrug transporter LmrP from Lactococcus lactis, using the pattern of distances between spin-label pairs previously shown to report on alternating access of the protein. We uncovered, at the molecular level, how the lipid headgroups shape the conformational-energy landscape of the transporter. The model emerging from our data suggests a direct interaction between lipid headgroups and a conserved motif of charged residues that control the conformational equilibrium through an interplay of electrostatic interactions within the protein. Together, our data lay the foundation for a comprehensive model of secondary multidrug transport in lipid bilayers.
Metadata
Item Type: | Article |
---|---|
Authors/Creators: |
|
Copyright, Publisher and Additional Information: | © 2016 Nature America, Inc. All rights reserved. This is an author produced version of a paper published in Nature Structural & Molecular Biology. Uploaded in accordance with the publisher's self-archiving policy. |
Dates: |
|
Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Biomedical Sciences (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 16 Jan 2017 16:13 |
Last Modified: | 16 Jan 2018 01:25 |
Published Version: | https://doi.org/10.1038/nsmb.3262 |
Status: | Published |
Publisher: | Nature Publishing Group |
Identification Number: | 10.1038/nsmb.3262 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:110585 |