Crystal structure of E. coli lipoprotein diacylglyceryl transferase
Copyright policy )Crystal structure of E. coli lipoprotein diacylglyceryl transferase
AbstractLipoprotein biogenesis is essential for bacterial survival. Phosphatidylglycerol:prolipoprotein diacylglyceryl transferase (Lgt) is an integral membrane enzyme that catalyses the first reaction of the three-step post-translational lipid modification. Deletion of the lgt gene is lethal to most Gram-negative bacteria. Here we present the crystal structures of Escherichia coli Lgt in complex with phosphatidylglycerol and the inhibitor palmitic acid at 1.9 and 1.6 Å resolution, respectively. The structures reveal the presence of two binding sites and support the previously reported structure–function relationships of Lgt. Complementation results of lgt-knockout cells with different mutant Lgt variants revealed critical residues, including Arg143 and Arg239, that are essential for diacylglyceryl transfer. Using a GFP-based in vitro assay, we correlated the activities of Lgt with structural observations. Together, the structural and biochemical data support a mechanism whereby substrate and product, lipid-modified lipobox-containing peptide, enter and leave the enzyme laterally relative to the lipid bilayer.
- University of Science and Technology of China China (People's Republic of)
- Institute of Biophysics China (People's Republic of)
- Anna University, Chennai India
- Chinese Academy of Sciences China (People's Republic of)
- University of Chinese Academy of Sciences China (People's Republic of)
Models, Molecular, Protein Conformation, Science, Lipoproteins, Q, Gene Expression Regulation, Bacterial, Article, Gene Expression Regulation, Enzymologic, Substrate Specificity, Transferases, Catalytic Domain, Escherichia coli, Crystallization, Gene Deletion, Protein Binding
Models, Molecular, Protein Conformation, Science, Lipoproteins, Q, Gene Expression Regulation, Bacterial, Article, Gene Expression Regulation, Enzymologic, Substrate Specificity, Transferases, Catalytic Domain, Escherichia coli, Crystallization, Gene Deletion, Protein Binding
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