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HYPOTHESIS AND THEORY article
Front. Mol. Biosci.
Sec. Lipids, Membranes and Membranous Organelles
Volume 11 - 2024 |
doi: 10.3389/fmolb.2024.1503709
Crystallographic Insights into Lipid-Membrane Protein Interactions in Microbial Rhodopsins
Provisionally accepted- 1 UMR5075 Institut de Biologie Structurale (IBS), Grenoble, France
- 2 European Synchrotron Radiation Facility, Grenoble, Rhône-Alpes, France
- 3 Structural Biochemistry (IBI-7), Institute of Biological Information processing, Julich Research Center, Helmholtz Association of German Research Centres (HZ), Jülich, North Rhine-Westphalia, Germany
The primary goal of our work is to provide structural insights into the influence of the hydrophobic lipid environment on the membrane proteins (MPs) structure and function. Our work will not cover the well-studied hydrophobic mismatch between the lipid bilayer and MPs. Instead, we will focus on the less-studied direct molecular interactions of lipids with the hydrophobic surfaces of MPs. To visualize the first layer of amphiphiles surrounding MPs and analyze their interaction with the proteins, we use the available highest-quality crystallographic structures of microbial rhodopsins. The results of the structure-based analysis allowed us to formulate the hypothetical concept of the role of the nearest layer of the lipids as an integral part of the MPs that are important for their structure and function. We then discuss how the lipid-MPs interaction is influenced by exogenous hydrophobic molecules, noble gases, which can compete with lipids for the surface of MPs and can be used in the systematic approach to verify the proposed concept experimentally. Finally, we raise the problems of currently available structural data that should be overcome to obtain a more profound picture of the lipid-MP interactions.
Keywords: Membrane Proteins, X-ray crystallogaphy, annular lipids, Detergent, Lipid cubic phase, Bicelles, Membrane Fusion, Oligomerization
Received: 29 Sep 2024; Accepted: 22 Oct 2024.
Copyright: © 2024 Bukhdruker, Melnikov, Baeken, Balandin and Gordeliy. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
* Correspondence:
Sergei Bukhdruker, UMR5075 Institut de Biologie Structurale (IBS), Grenoble, France
Igor Melnikov, European Synchrotron Radiation Facility, Grenoble, Rhône-Alpes, France
Christian Baeken, Structural Biochemistry (IBI-7), Institute of Biological Information processing, Julich Research Center, Helmholtz Association of German Research Centres (HZ), Jülich, 52428, North Rhine-Westphalia, Germany
Taras Balandin, Structural Biochemistry (IBI-7), Institute of Biological Information processing, Julich Research Center, Helmholtz Association of German Research Centres (HZ), Jülich, 52428, North Rhine-Westphalia, Germany
Valentin Gordeliy, UMR5075 Institut de Biologie Structurale (IBS), Grenoble, France
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