ArticleNature communications2022
Cryo-EM structures of a LptDE transporter in complex with Pro-macrobodies offer insight into lipopolysaccharide translocation.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 55 citations in OpenAlex.
- Structural and mechanistic insights into the constitutive Themis-Grb2 complex in T cell signalling.Nature communications · 2026Article
- Integration of Membrane Proteins into the Outer Membrane of Diderm Bacteria by the BAM Complex.Chemical reviews · 2026Review
- Resolution of a T1-Like Bacteriophage Outbreak by Receptor Engineering.Molecular biotechnology · 2026Article
- Designing Rigid Protein Fiducials to Visualize GPCR Conformational States.bioRxiv : the preprint server for biology · 2026Article
- Differential membrane lipid disruption by lipopeptide antibiotics, colistin and turnercyclamycins.Nature communications · 2026Article
- Hidden gems bring proteins into view.Nature chemical biology · 2026Article
- Involvement of hcp2 on maintaining cell wall integrity and pathogenicity of Vibrio alginolyticus by modulating Sec pathway.The Biochemical journal · 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
- The structure of the bacterial outer membrane transporter FusA enabled by addition of the native lipid lipopolysaccharide.Journal of structural biology: X · 2025Article
- Structural basis of lipopolysaccharide assembly by the outer membrane translocon holo-complex.Nature communications · 2025Article
- Dynamic TOM-TIM23 supercomplex directs mitochondrial protein translocation and sorting.Nature structural & molecular biology · 2025Article
- High-Throughput Identification and Characterization of LptDE-Binding Bicycle Peptides Using Phage Display and Cryo-EM.Journal of medicinal chemistry · 2025Article
- Selection of nanobodies against liponanoparticle-embedded membrane proteins by yeast-surface display.Protein science : a publication of the Protein Society · 2025Article
- Conformational Plasticity of LptC Regulates Lipopolysaccharide Transport by the LptBJournal of the American Chemical Society · 2025Article
- Analysis ofmSphere · 2025Article
- Disulfide-constrained Fabs overcome target size limitation for high-resolution single particle cryoEM.Nature communications · 2025Article
- Inhibiting Lipopolysaccharide Biogenesis: The More You Know the Further You Go.Annual review of biochemistry · 2025Review
- Surface lipoprotein sorting by crosstalk between Lpt and Lol pathways in gram-negative bacteria.Nature communications · 2025Article
- Structures of native SV2A reveal the binding mode for tetanus neurotoxin and anti-epileptic racetams.Nature communications · 2025Article
- Molecular basis of pyruvate transport and inhibition of the human mitochondrial pyruvate carrier.Science advances · 2025Article
Corrections and comments
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Authors and funding
14 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipopolysaccharides are major constituents of the extracellular leaflet in the bacterial outer membrane and form an effective physical barrier for environmental threats and for antibiotics in Gram-negative bacteria. The last step of LPS insertion via the Lpt pathway is mediated by the LptD/E protein complex. Detailed insights into the architecture of LptDE transporter complexes have been derived from X-ray crystallography. However, no structure of a laterally open LptD transporter, a transient state that occurs during LPS release, is available to date. Here, we report a cryo-EM structure of a partially opened LptDE transporter in complex with rigid chaperones derived from nanobodies, at 3.4 Å resolution. In addition, a subset of particles allows to model a structure of a laterally fully opened LptDE complex. Our work offers insights into the mechanism of LPS insertion, provides a structural framework for the development of antibiotics targeting LptD and describes a highly rigid chaperone scaffold to enable structural biology of challenging protein targets.
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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.