Phosphatidylglyerol Lipid Binding at the Active Site of an Intramembrane Protease.

The Journal of Membrane Biology
Ana-Nicoleta Bondar

Abstract

Transmembrane substrate cleavage by the small Escherichia coli rhomboid protease GlpG informs on mechanisms by which lipid interactions shape reaction coordinates of membrane-embedded enzymes. Here, I review and discuss new work on the molecular picture of protein-lipid interactions that might govern the formation of the substrate-enzyme complex in fluid lipid membranes. Negatively charged PG-type lipids are of particular interest, because they are a major component of bacterial membranes. Atomistic computer simulations indicate POPG and DOPG lipids bridge remote parts of GlpG and might pre-occupy the substrate-docking site. Inhibition of catalytic activity by PG lipids could arise from ligand-like lipid binding at the active site, which could delay or prevent substrate docking. Dynamic protein-lipid H-bond networks, water access to the active site, and fluctuations in the orientation of GlpG suggest that GlpG has lipid-coupled dynamics that could shape the energy landscape of transmembrane substrate docking.

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Citations

May 28, 2021·The Journal of Membrane Biology·Thomas PucadyilDurba Sengupta

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Methods Mentioned

BETA
X-ray

Software Mentioned

VMD
Bridge
Clustal Omega
CHARMM
POPG
CHARMM36
tcl
DOPG
GUI

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