ArticleNature communications2021
Mechanism of LolCDE as a molecular extruder of bacterial triacylated lipoproteins.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 71 citations in OpenAlex.
- Mechanistic basis of LolDF-mediated lipoprotein transport in Acinetobacter.Nature communications · 2026Article
- Conformational hijacking of lipoprotein transporter LolDF enables precision antimicrobial activity against Acinetobacter baumannii.Nature communications · 2026Article
- Leveraging the lipoprotein trafficking pathway for the development of novel antimicrobials.RSC chemical biology · 2026Review
- Structure and druggable conformation of the homodimeric lipoprotein transporter of Acinetobacter baumannii.Nature communications · 2026Article
- Borrelia BBJ25 is a plasmid-encoded Omp85-family protein associated with a potential export system.Bioscience reports · 2026Article
- Molecular mechanism of action of small molecule SMT-738 on bacterial lipoprotein transporter LolCDE.Nature communications · 2026Article
- Identification and characterization of the functional LolB ortholog inbioRxiv : the preprint server for biology · 2026Article
- Liganded LolCDE structures reveal a common substrate-LolE interaction guiding bacterial lipoprotein transport.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Structural basis of outer membrane biogenesis by the TamAB translocase.Nature communications · 2026Article
- Structural analysis of a Gram-positive type VII ABC transporter induced by cell wall-targeting antibiotics.Structure (London, England : 1993) · 2026Article
- How to spare gut microbiota from antibiotic effects? PK-PD based innovative strategies, target specificity, and molecule-to-medicinal properties.RSC medicinal chemistry · 2025Review
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- Advances in Small Molecule Inhibitors Targeting the Bacterial Lipoprotein Transport System (Lol) in Gram-Negative Bacteria.Chemistry, an Asian journal · 2025Review
- Global health perspectives on antibacterial drug discovery and the preclinical pipeline.Nature reviews. Microbiology · 2025Review
- Conformational cycle and small-molecule inhibition mechanism of a plant ABCB transporter in lipid membranes.Science advances · 2025Article
- Surface lipoprotein sorting by crosstalk between Lpt and Lol pathways in gram-negative bacteria.Nature communications · 2025Article
- Cryo-EM of human P-glycoprotein reveals an intermediate occluded conformation during active drug transport.Nature communications · 2025Article
- Novel Antibacterial Approaches and Therapeutic Strategies.Antibiotics (Basel, Switzerland) · 2025Review
- Genetic engineering of RuBisCO by multiplex CRISPR editing small subunits in rice.Plant biotechnology journal · 2025Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipoproteins are important for bacterial growth and antibiotic resistance. These proteins use lipid acyl chains attached to the N-terminal cysteine residue to anchor on the outer surface of cytoplasmic membrane. In Gram-negative bacteria, many lipoproteins are transported to the outer membrane (OM), a process dependent on the ATP-binding cassette (ABC) transporter LolCDE which extracts the OM-targeted lipoproteins from the cytoplasmic membrane. Lipid-anchored proteins pose a unique challenge for transport machinery as they have both hydrophobic lipid moieties and soluble protein component, and the underlying mechanism is poorly understood. Here we determined the cryo-EM structures of nanodisc-embedded LolCDE in the nucleotide-free and nucleotide-bound states at 3.8-Å and 3.5-Å resolution, respectively. The structural analyses, together with biochemical and mutagenesis studies, uncover how LolCDE recognizes its substrate by interacting with the lipid and N-terminal peptide moieties of the lipoprotein, and identify the amide-linked acyl chain as the key element for LolCDE interaction. Upon nucleotide binding, the transmembrane helices and the periplasmic domains of LolCDE undergo large-scale, asymmetric movements, resulting in extrusion of the captured lipoprotein. Comparison of LolCDE and MacB reveals the conserved mechanism of type VII ABC transporters and emphasizes the unique properties of LolCDE as a molecule extruder of triacylated lipoproteins.
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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.