5AZC

Crystal structure of Escherichia coli Lgt in complex with phosphatidylglycerol

Summary for 5AZC

• Entry DOI: 10.2210/pdb5azc/pdb
• Related: 5azb
• Descriptor: Prolipoprotein diacylglyceryl transferase, (1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE (3 entities in total)
• Functional Keywords: inhibitor, complex, transferase
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane ; Multi- pass membrane protein : P60955
• Total number of polymer chains: 1
• Total formula weight: 41814.30

Authors

Zhang, X.C.,Mao, G.,Zhao, Y. (deposition date: 2015-09-30, release date: 2016-01-27, Last modification date: 2024-03-20)

Primary citation

Mao, G.,Zhao, Y.,Kang, X.,Li, Z.,Zhang, Y.,Wang, X.,Sun, F.,Sankaran, K.,Zhang, X.C.
Crystal structure of E. coli lipoprotein diacylglyceryl transferase
Nat Commun, 7:10198-10198, 2016

PubMed Abstract: Lipoprotein 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.

PubMed: 26729647
DOI: 10.1038/ncomms10198

Experimental method

X-RAY DIFFRACTION (1.902 Å)