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Allosteric coupling between a lipid bilayer and a membrane protein.

Clarisse Fourel1, Yanna Gautier2, Alexandre Pozza3

  • 1Institut de Chimie des Substances Naturelles, CNRS, Université Paris-Saclay, Gif-sur-Yvette, France; Laboratoire de Biochimie des Protéines Membranaires, Université Paris Cité, CNRS, Paris, France.

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Membrane protein OmpX liquefies surrounding lipids, delaying membrane gelation. This interaction unexpectedly alters the protein core, revealing a new allosteric pathway in biological membranes.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Membrane Biology

Background:

  • Biological membrane functions depend on dynamic lipid-protein interactions.
  • Understanding these interactions is crucial for deciphering cellular processes.

Purpose of the Study:

  • To elucidate the atomic-scale allosteric communication between a lipid bilayer and the membrane protein OmpX.
  • To investigate how lipid dynamics influence membrane protein structure and function.

Main Methods:

  • High-pressure Nuclear Magnetic Resonance (NMR) of lipid nanodiscs.
  • All-atom molecular dynamics (MD) simulations.
  • Integration of experimental and computational approaches.

Main Results:

  • OmpX delays lipid bilayer gelation by liquefying the annular lipid shell via hydrophobic and roughness matching.
  • Changes in lipid bilayer mechanical properties affect amino acid side chain energetics at the protein interface and within the protein core.
  • Identified a thermodynamically coupled but kinetically uncoupled allosteric pathway.

Conclusions:

  • Lipid-protein allostery involves a pathway linking lipid dynamics to the membrane protein interior.
  • This finding impacts the fundamental understanding of biological membrane function.
  • Highlights the intricate relationship between membrane mechanics and protein behavior.