ArticleNature communications2016
Crystal structure of E. coli lipoprotein diacylglyceryl transferase.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 93 citations in OpenAlex.
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- Uncovering the prevalence, key biogenesis enzymes, and biological significance of archaeal lipoproteins.Nature communications · 2025Article
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- Selection Maintains Photosynthesis in a Symbiotic Cyanobacterium Despite Redundancy With its Fern Host.Molecular biology and evolution · 2025Article
- Outer membrane lipoproteins: late to the party, but the center of attention.Journal of bacteriology · 2025Review
- Lipoprotein Signal Peptide as Adjuvants: Leveraging Lipobox-Driven TLR2 Activation in Modern Vaccine Design.Vaccines · 2025Review
- Deciphering the molecular basis of lipoprotein recognition and transport by LolCDE.Signal transduction and targeted therapy · 2024Article
- A screen for cell envelope stress uncovers an inhibitor of prolipoprotein diacylglyceryl transferase, Lgt, iniScience · 2024Article
- Fatty acids ofMicrobiology spectrum · 2024Article
- Reducing gut microbiome-driven adipose tissue inflammation alleviates metabolic syndrome.Microbiome · 2023Article
- Using the inner membrane ofEngineering in life sciences · 2023Article
- Making a chink in their armor: Current and next-generation antimicrobial strategies against the bacterial cell envelope.Advances in microbial physiology · 2023Article
- Cryo-EM structures of LolCDE reveal the molecular mechanism of bacterial lipoprotein sorting in Escherichia coli.PLoS biology · 2022Article
- Yields and Immunomodulatory Effects of Pneumococcal Membrane Vesicles Differ with the Bacterial Growth Phase.Advanced healthcare materials · 2022Article
- Breaking down the cell wall: Still an attractive antibacterial strategy.Frontiers in microbiology · 2022Review
- Production of extracellular lipase from psychrotrophic bacterium Oceanisphaera sp. RSAP17 isolated from arctic soil.Antonie van Leeuwenhoek · 2021Article
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.