Structural Research of Diacylglyceryl Transferases

The biosynthetic pathway for bacterial lipoproteins, which is essential for bacterial survival, involves three reactions catalyzed by different enzymes. The first reaction is catalyzed by the membrane enzyme diacylglyceryl transferase (Lgt), which recognizes the lipobox motif in pre-prolipoproteins and transfers a diacylglyceryl group from phosphatidylglycerol to the conserved cysteine residue in the motif. The crystal structures of Escherichia coli Lgt with lipid ligands revealed a laterally opening central cavity with the active site and two binding sites for phosphatidylglycerol, the donor substrate. The structures also supported previous structure-function relationships of Lgt and identified critical residues, including Arg143 and Arg239, essential for diacylglyceryl transfer. Mutagenesis and in vitro studies identified critical residues essential for diacylglyceryl transfer and suggested a feasible mechanism of substrate recognition.

These studies of Lgt structure and the biosynthetic pathway for bacterial lipoproteins are crucial for understanding the fundamental biological functions of these molecules and developing new antibiotics to combat bacterial infections.

Figure 1. The overall structure of EcLgt. (Mao G, et al., 2016)

Table 1. Structural Research of Diacylglyceryl Transferases.

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Reference

1. Mao G, et al. Crystal structure of E. coli lipoprotein diacylglyceryl transferase. Nature Communications. 2016, 7(1): 10198.