ArticleNature chemical biology2020
Structural insight into the formation of lipoprotein-β-barrel complexes.
Article in Nature chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 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.
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Who cites it
37 citing papers in PubMed, 50 citations in OpenAlex.
- Computational systems immunology and multi-scale modeling for the design of a Multi-Epitope Vaccine (MEV) against emerging multidrug-resistant Klebsiella michiganensis.International microbiology : the official journal of the Spanish Society for Microbiology · 2026Article
- Structural and functional insights into the Rcs phosphorelay.bioRxiv : the preprint server for biology · 2026Article
- Mechanism of phospholipid transport to the bacterial outer membrane by TAM.bioRxiv : 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
- Protein-Protein Interactions as Promising Molecular Targets for Novel Antimicrobials Aimed at Gram-Negative Bacteria.International journal of molecular sciences · 2025Review
- Structure of a distinct β-barrel assembly machinery complex in the Bacteroidota.Nature microbiology · 2025Article
- Molecular insights into how the motions of the β-barrel and POTRA domains of BamA are coupled for efficient function.Nature communications · 2025Article
- Bacterial cell widening alters periplasmic size and activates envelope stress responses.The EMBO journal · 2025Article
- Article
- A bipartite bacterial virulence factor targets the complement system and neutrophil activation.The EMBO journal · 2025Article
- Breaking Barriers: Exploiting Envelope Biogenesis and Stress Responses to Develop Novel Antimicrobial Strategies in Gram-Negative Bacteria.Pathogens (Basel, Switzerland) · 2024Review
- ATP-independent assembly machinery of bacterial outer membranes: BAM complex structure and function set the stage for next-generation therapeutics.Protein science : a publication of the Protein Society · 2024Review
- Lateral gating mechanism and plasticity of the β-barrel assembly machinery complex in micelles andPNAS nexus · 2024Article
- Designing of a multi-epitopes based vaccine againstFrontiers in immunology · 2024Article
- Altering Escherichia coli envelope integrity by mimicking the lipoprotein RcsF.Archives of microbiology · 2023Article
- NlpE Is an OmpA-Associated Outer Membrane Sensor of the Cpx Envelope Stress Response.Journal of bacteriology · 2023Article
- Envelope-Stress Sensing Mechanism of Rcs and Cpx Signaling Pathways in Gram-Negative Bacteria.Journal of microbiology (Seoul, Korea) · 2023Review
- Teasing apart the evolution of lipoprotein trafficking in gram-negative bacteria reveals a bifunctional LolA.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Adaptive Evolution Compensated for the Plasmid Fitness Costs Brought by Specific Genetic Conflicts.Pathogens (Basel, Switzerland) · 2023Article
- Detecting Lipoproteins Sneaking Out of the Lipopolysaccharide Leaflet.Methods in molecular biology (Clifton, N.J.) · 2022Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 3 countries.
Funding
Abstract
The β-barrel assembly machinery (BAM) inserts outer membrane β-barrel proteins (OMPs) in the outer membrane of Gram-negative bacteria. In Enterobacteriacea, BAM also mediates export of the stress sensor lipoprotein RcsF to the cell surface by assembling RcsF-OMP complexes. Here, we report the crystal structure of the key BAM component BamA in complex with RcsF. BamA adopts an inward-open conformation, with the lateral gate to the membrane closed. RcsF is lodged deep within the lumen of the BamA barrel, binding regions proposed to undergo outward and lateral opening during OMP insertion. On the basis of our structural and biochemical data, we propose a push-and-pull model for RcsF export following conformational cycling of BamA, and provide a mechanistic explanation for how RcsF uses its interaction with BamA to detect envelope stress. Our data also suggest that the flux of incoming OMP substrates is involved in the control of BAM activity.
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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.