Crystal structure and biochemical characterization of the transmembrane PAP2 type phosphatidylglycerol phosphate phosphatase from Bacillus subtilis |
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Authors: | Meriem El Ghachi Nicole Howe Rodolphe Auger Alexandre Lambion Annick Guiseppi François Delbrassine Guillaume Manat Sophie Roure Sabine Peslier Eric Sauvage Lutz Vogeley Juan-Carlos Rengifo-Gonzalez Paulette Charlier Dominique Mengin-Lecreulx Maryline Foglino Thierry Touzé Martin Caffrey Frédéric Kerff |
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Affiliation: | 1.Centre d’Ingénierie des Protéines, InBioS,Université de Liège,Liège,Belgium;2.Membrane Structural and Functional Biology Group,Schools of Medicine and Biochemistry and Immunology, Trinity College Dublin,Dublin 2,Ireland;3.Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS,Univ Paris-Sud, Université Paris-Saclay,Gif-sur-Yvette cedex,France;4.Laboratoire de Chimie Bactérienne UMR 7283,Aix-Marseille Université,Marseille,France |
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Abstract: | Type 2 phosphatidic acid phosphatases (PAP2s) can be either soluble or integral membrane enzymes. In bacteria, integral membrane PAP2s play major roles in the metabolisms of glycerophospholipids, undecaprenyl-phosphate (C55-P) lipid carrier and lipopolysaccharides. By in vivo functional experiments and biochemical characterization we show that the membrane PAP2 coded by the Bacillus subtilis yodM gene is the principal phosphatidylglycerol phosphate (PGP) phosphatase of B. subtilis. We also confirm that this enzyme, renamed bsPgpB, has a weaker activity on C55-PP. Moreover, we solved the crystal structure of bsPgpB at 2.25 Å resolution, with tungstate (a phosphate analog) in the active site. The structure reveals two lipid chains in the active site vicinity, allowing for PGP substrate modeling and molecular dynamic simulation. Site-directed mutagenesis confirmed the residues important for substrate specificity, providing a basis for predicting the lipids preferentially dephosphorylated by membrane PAP2s. |
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