ArticleNature communications2017
Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 69 citations in OpenAlex.
- Reconstitution of the LnsAB lipoprotein N-acylation system complex from Staphylococcus aureus and characterization of substrate preference.The Journal of biological chemistry · 2026Article
- Cytosolic CTH senses bacterial lipoproteins and drives noncanonical inflammasome activation.Nature immunology · 2026Article
- Bacterial post-translational changes: the possible enigma of multidrug resistance.Archives of microbiology · 2026Review
- Article
- Surface protein machineries in Gram-negative bacteria.Journal of cell science · 2025Review
- Advances in Small Molecule Inhibitors Targeting the Bacterial Lipoprotein Transport System (Lol) in Gram-Negative Bacteria.Chemistry, an Asian journal · 2025Review
- Heterologous protein exposure and secretion optimization in Mycoplasma pneumoniae.Microbial cell factories · 2024Article
- Identification and characterization of the lipoproteinProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Breaking Barriers: Exploiting Envelope Biogenesis and Stress Responses to Develop Novel Antimicrobial Strategies in Gram-Negative Bacteria.Pathogens (Basel, Switzerland) · 2024Review
- Identification and Characterization of the LipoproteinbioRxiv : the preprint server for biology · 2024Article
- Computational Design of Cyclic Peptide Inhibitors of a Bacterial Membrane Lipoprotein Peptidase.ACS chemical biology · 2024Article
- Fatty acids ofMicrobiology spectrum · 2024Article
- 7.10 MAG. A Novel Host Monoacylglyceride forCrystal growth & design · 2024Article
- ProTInSeq: transposon insertion tracking by ultra-deep DNA sequencing to identify translated large and small ORFs.Nature communications · 2024Article
- Structure snapshots reveal the mechanism of a bacterial membrane lipoproteinScience advances · 2023Article
- Making a chink in their armor: Current and next-generation antimicrobial strategies against the bacterial cell envelope.Advances in microbial physiology · 2023Article
- Machine Learning and Computational Chemistry for the Endocannabinoid System.Methods in molecular biology (Clifton, N.J.) · 2023Review
- Cryo-EM structures of LolCDE reveal the molecular mechanism of bacterial lipoprotein sorting in Escherichia coli.PLoS biology · 2022Article
- Breaking down the cell wall: Still an attractive antibacterial strategy.Frontiers in microbiology · 2022Review
- CG2AT2: an Enhanced Fragment-Based Approach for Serial Multi-scale Molecular Dynamics Simulations.Journal of chemical theory and computation · 2021Article
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipoproteins serve essential roles in the bacterial cell envelope. The posttranslational modification pathway leading to lipoprotein synthesis involves three enzymes. All are potential targets for the development of new antibiotics. Here we report the crystal structure of the last enzyme in the pathway, apolipoprotein N-acyltransferase, Lnt, responsible for adding a third acyl chain to the lipoprotein's invariant diacylated N-terminal cysteine. Structures of Lnt from Pseudomonas aeruginosa and Escherichia coli have been solved; they are remarkably similar. Both consist of a membrane domain on which sits a globular periplasmic domain. The active site resides above the membrane interface where the domains meet facing into the periplasm. The structures are consistent with the proposed ping-pong reaction mechanism and suggest plausible routes by which substrates and products enter and leave the active site. While Lnt may present challenges for antibiotic development, the structures described should facilitate design of therapeutics with reduced off-target effects.
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