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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. [Image: see text]
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10.1007/s00232-020-00152-z
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document_parses/pdf_json/b4ab00f7d40b9290be75ba3868b991adb412629b.json
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document_parses/pmc_json/PMC7688093.xml.json
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Phosphatidylglyerol Lipid Binding at the Active Site of an Intramembrane Protease
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