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Identification and assessment of cardiolipin interactions with E. coli inner membrane proteins

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Corey, Robin A., Song, Wanling, Duncan, Anna L., Ansell, T. Bertie, Sansom, Mark S. P. and Stansfeld, Phillip J. (2021) Identification and assessment of cardiolipin interactions with E. coli inner membrane proteins. Science Advances, 7 (34). eabh2217. doi:10.1126/sciadv.abh2217 ISSN 2375-2548.

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Official URL: https://doi.org/10.1126/sciadv.abh2217

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Abstract

Integral membrane proteins are localized and/or regulated by lipids present in the surrounding bilayer. While bacteria have relatively simple membranes, there is ample evidence that many bacterial proteins bind to specific lipids, especially the anionic lipid cardiolipin. Here, we apply molecular dynamics simulations to assess lipid binding to 42 different Escherichia coli inner membrane proteins. Our data reveal an asymmetry between the membrane leaflets, with increased anionic lipid binding to the inner leaflet regions of the proteins, particularly for cardiolipin. From our simulations, we identify >700 independent cardiolipin binding sites, allowing us to identify the molecular basis of a prototypical cardiolipin binding site, which we validate against structures of bacterial proteins bound to cardiolipin. This allows us to construct a set of metrics for defining a high-affinity cardiolipin binding site on bacterial membrane proteins, paving the way for a heuristic approach to defining other protein-lipid interactions.

Item Type: Journal Article
Subjects: Q Science > QP Physiology
Divisions: Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- )
Library of Congress Subject Headings (LCSH): Cardiolipin, Membrane proteins, Lipids, Escherichia coli
Journal or Publication Title: Science Advances
Publisher: American Association for the Advancement of Science
ISSN: 2375-2548
Official Date: 20 August 2021
Dates:
DateEvent
20 August 2021Published
30 June 2021Accepted
Volume: 7
Number: 34
Article Number: eabh2217
DOI: 10.1126/sciadv.abh2217
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access (Creative Commons)
Date of first compliant deposit: 23 August 2021
Date of first compliant Open Access: 24 August 2021
RIOXX Funder/Project Grant:
Project/Grant IDRIOXX Funder NameFunder ID
208361/Z/17/ZWellcome Trusthttp://dx.doi.org/10.13039/100010269
UNSPECIFIEDBiotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
DPhil studentshipWellcome Trusthttp://dx.doi.org/10.13039/100010269
UNSPECIFIEDEngineering and Physical Sciences Research Councilhttp://dx.doi.org/10.13039/501100000266
MR/S009213/1Medical Research Councilhttp://dx.doi.org/10.13039/501100000265
BB/P01948X/1 Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
BB/R002517/1 Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
BB/S003339/1Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
EP/L000253/1Engineering and Physical Sciences Research Councilhttp://dx.doi.org/10.13039/501100000266
EP/P020232/1Engineering and Physical Sciences Research Councilhttp://dx.doi.org/10.13039/501100000266

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