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Journal Articles Biochimica et Biophysica Acta:Biomembranes Year : 2022

Lipid-membrane protein interaction visualized by cryo-EM: a review

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Abstract

Membrane proteins reside at interfaces between aqueous and lipid media and solving their molecular structure relies most of the time on removing them from the membrane using detergent. Luckily, this solubilization process does not strip them from all the associated lipids and single-particle cryotransmission electron microscopy (SP-TEM) has proved a very good tool to visualize both protein high-resolution structure and, often, many of its associated lipids. In this review, we observe membrane protein structures from the Protein DataBank and their associated maps in the Electron Microscopy DataBase and determine how the SP-TEM maps allow lipid visualization, the type of binding sites, the influence of symmetry, resolution and other factors. We illustrate lipid visualization around and inside the protein core, show that some lipid bilayers in the core can be shifted with respect to the membrane and how some proteins can actively bend the lipid bilayer that binds to them. We conclude that resolution improvement in SP-TEM will likely enable many more discoveries regarding the role of lipids bound to proteins.
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Dates and versions

hal-03808058 , version 1 (10-10-2022)

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Valérie Biou. Lipid-membrane protein interaction visualized by cryo-EM: a review. Biochimica et Biophysica Acta:Biomembranes, 2022, ⟨10.1016/j.bbamem.2022.184068⟩. ⟨hal-03808058⟩
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