ArticleNature communications2017
Crystal structure of E. coli apolipoprotein N-acyl transferase.
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 22 papers.
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Who cites it
22 citing papers in PubMed.
- Mechanistic basis of LolDF-mediated lipoprotein transport in Acinetobacter.Nature communications · 2026Article
- Impact of the 294 bp SINE Insertion in 5'UTR of theAnimals : an open access journal from MDPI · 2025Article
- Identification and characterization of the lipoproteinProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Identification and Characterization of the LipoproteinbioRxiv : the preprint server for biology · 2024Article
- Fatty acids ofMicrobiology spectrum · 2024Article
- Structure snapshots reveal the mechanism of a bacterial membrane lipoproteinScience advances · 2023Article
- Review
- 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
- Structural basis of the membrane intramolecular transacylase reaction responsible for lyso-form lipoprotein synthesis.Nature communications · 2021Article
- Mode of action of lipoprotein modification enzymes-Novel antibacterial targets.Molecular microbiology · 2021Review
- Bacterial Lipoprotein Posttranslational Modifications. New Insights and Opportunities for Antibiotic and Vaccine Development.Frontiers in microbiology · 2021Review
- Structure and Mechanism of DHHC Protein Acyltransferases.Journal of molecular biology · 2020Review
- Characterization of a novel AraC/XylS-regulated family of N-acyltransferases in pathogens of the order Enterobacterales.PLoS pathogens · 2020Article
- Article
- DHHC20 Palmitoyl-Transferase Reshapes the Membrane to Foster Catalysis.Biophysical journal · 2020Article
- Conformational changes in Apolipoprotein N-acyltransferase (Lnt).Scientific reports · 2020Article
- Evidence to Suggest Bacterial Lipoprotein Diacylglyceryl Transferase (Lgt) is a Weakly Associated Inner Membrane Protein.The Journal of membrane biology · 2019Article
- A sensitive fluorescence-based assay to monitor enzymatic activity of the essential integral membrane protein Apolipoprotein N-acyltransferase (Lnt).Scientific reports · 2019Article
- Structural and Functional Characterization of the BcsG Subunit of the Cellulose Synthase in Salmonella typhimurium.Journal of molecular biology · 2018Article
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Gram-negative bacteria, lipid modification of proteins is catalysed in a three-step pathway. Apolipoprotein N-acyl transferase (Lnt) catalyses the third step in this pathway, whereby it transfers an acyl chain from a phospholipid to the amine group of the N-terminal cysteine residue of the apolipoprotein. Here, we report the 2.6-Å crystal structure of Escherichia coli Lnt. This enzyme contains an exo-membrane nitrilase domain fused to a transmembrane (TM) domain. The TM domain of Lnt contains eight TM helices which form a membrane-embedded cavity with a lateral opening and a periplasmic exit. The nitrilase domain is located on the periplasmic side of the membrane, with its catalytic cavity connected to the periplasmic exit of the TM domain. An amphipathic lid loop from the nitrilase domain interacts with the periplasmic lipid leaflet, forming an interfacial entrance from the lipid bilayer to the catalytic centre for both the lipid donor and acceptor substrates.
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