ArticleNature2016
Structural basis of outer membrane protein insertion by the BAM complex.
Article in Nature, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 195 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.
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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
195 citing papers in PubMed, 311 citations in OpenAlex.
- Article
- In vitro reconstitution implicates multiple OMP assembly factors in CdiAThe Journal of biological chemistry · 2026Article
- Cryo-EM structures of the SurA-BAM complex reveal conformational changes in outer membrane protein assembly.Nature communications · 2026Article
- 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
- L-type pyocins inhibit the BAM complex to kill without cell entry.Nature communications · 2026Article
- DeepPath: overcoming data scarcity for protein transition pathway prediction using physics-based deep learning.Chemical science · 2026Article
- Monitoring Membrane Protein Folding Assisted by Insertases and Translocases Using AFM-Based Single-Molecule Force Spectroscopy.Chemical reviews · 2026Review
- A mechanism for substrate quality control in outer membrane protein assembly.Proceedings of the National Academy of Sciences of the United States of America · 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
- Bacterial cell envelope-targeting antibiotics.Nature reviews. Microbiology · 2026Review
- Article
- 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
- A fluorescent reporter and single-turnover kinetics reveal insight into BAM complex function.Proceedings of the National Academy of Sciences of the United States of America · 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
- Insights into the complex formation of a trimeric autotransporter adhesin with a peptidoglycan-binding periplasmic protein.Cell surface (Amsterdam, Netherlands) · 2025Article
- The dynamic lateral gate of the mitochondrial β-barrel biogenesis machinery is blocked by darobactin A.Nature communications · 2025Article
135 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 7 institutions in 2 countries.
Funding
Abstract
All Gram-negative bacteria, mitochondria and chloroplasts have outer membrane proteins (OMPs) that perform many fundamental biological processes. The OMPs in Gram-negative bacteria are inserted and folded into the outer membrane by the β-barrel assembly machinery (BAM). The mechanism involved is poorly understood, owing to the absence of a structure of the entire BAM complex. Here we report two crystal structures of the Escherichia coli BAM complex in two distinct states: an inward-open state and a lateral-open state. Our structures reveal that the five polypeptide transport-associated domains of BamA form a ring architecture with four associated lipoproteins, BamB-BamE, in the periplasm. Our structural, functional studies and molecular dynamics simulations indicate that these subunits rotate with respect to the integral membrane β-barrel of BamA to induce movement of the β-strands of the barrel and promote insertion of the nascent OMP.
Indexed as
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What OpenQuestion holds
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.