ArticleNature2014
Structural basis for lipopolysaccharide insertion in the bacterial outer membrane.
Article in Nature, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 171 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
171 citing papers in PubMed, 277 citations in OpenAlex.
- Article
- Interactions of outer membrane lipoproteins Pseudomonas aeruginosa PA3214 and Escherichia coli PqiC with their MCE protein binding partners, PA3213 and PqiB.The Journal of biological chemistry · 2026Article
- Integration of Membrane Proteins into the Outer Membrane of Diderm Bacteria by the BAM Complex.Chemical reviews · 2026Review
- Structures of folding intermediates on BAM show diverse substrates fold by a conserved mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Peptoid-based antimicrobial strategies against polymyxin-resistant Gram-negative bacteria.Journal of applied microbiology · 2026Article
- Molecular mechanism of action of small molecule SMT-738 on bacterial lipoprotein transporter LolCDE.Nature communications · 2026Article
- Phospholipid composition strongly affects the assembly of β barrel proteins into purified bacterial outer membranes.Nature communications · 2026Article
- Structural basis of outer membrane biogenesis by the TamAB translocase.Nature communications · 2026Article
- From gatekeepers to mitochondrial mischief: how bacterial outer membrane proteins crash the host cell party.FEMS microbiology reviews · 2026Review
- Structural snapshots of Pseudomonas aeruginosa LptBNature communications · 2025Article
- Article
- Identification of Genetic and Environmental Factors Suppressing the Lethality and Antibiotic Susceptibility Mediated by Depletion of LptD, a Lipopolysaccharide Transport Protein.Journal of microbiology and biotechnology · 2025Article
- Small siphophage binding to an open state of the LptDE outer membrane lipopolysaccharide translocon.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural basis of lipopolysaccharide assembly by the outer membrane translocon holo-complex.Nature communications · 2025Article
- High-Throughput Identification and Characterization of LptDE-Binding Bicycle Peptides Using Phage Display and Cryo-EM.Journal of medicinal chemistry · 2025Article
- 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
- Adaptive genetics reveals constraints on protein structure/function by evolving E. coli under constant nutrient limitation.BMC biology · 2025Article
- Inhibiting Lipopolysaccharide Biogenesis: The More You Know the Further You Go.Annual review of biochemistry · 2025Review
111 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
One of the fundamental properties of biological membranes is the asymmetric distribution of membrane lipids. In Gram-negative bacteria, the outer leaflet of the outer membrane is composed predominantly of lipopolysaccharides (LPS). The export of LPS requires seven essential lipopolysaccharide transport (Lpt) proteins to move LPS from the inner membrane, through the periplasm to the surface. Of the seven Lpt proteins, the LptD-LptE complex is responsible for inserting LPS into the external leaflet of the outer membrane. Here we report the crystal structure of the ∼110-kilodalton membrane protein complex LptD-LptE from Shigella flexneri at 2.4 Å resolution. The structure reveals an unprecedented two-protein plug-and-barrel architecture with LptE embedded into a 26-stranded β-barrel formed by LptD. Importantly, the secondary structures of the first two β-strands are distorted by two proline residues, weakening their interactions with neighbouring β-strands and creating a potential portal on the barrel wall that could allow lateral diffusion of LPS into the outer membrane. The crystal structure of the LptD-LptE complex opens the door to new antibiotic strategies targeting the bacterial outer membrane.
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Registered trials
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.