ArticleNature communications2019
Bacterial outer membrane proteins assemble via asymmetric interactions with the BamA β-barrel.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.
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Who cites it
84 citing papers in PubMed.
- Cryo-EM structures of monomeric and dimeric human SAM complexes.Cell research · 2026Article
- L-type pyocins inhibit the BAM complex to kill without cell entry.Nature communications · 2026Article
- 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
- The BaeSR two-component system activatesmBio · 2026Article
- Integration of Membrane Proteins into the Outer Membrane of Diderm Bacteria by the BAM Complex.Chemical reviews · 2026Review
- 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
- Structural insights into outer membrane protein biogenesis in pathogenic Neisseria.Structure (London, England : 1993) · 2025Article
- Molecular insights into how the motions of the β-barrel and POTRA domains of BamA are coupled for efficient function.Nature communications · 2025Article
- Antibacterial macrocyclic peptides reveal a distinct mode of BamA inhibition.Nature communications · 2025Article
- Architecture and conformational dynamics of the BAM-SurA holo insertase complex.Science advances · 2025Article
- Article
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- Terrabacteria: redefining bacterial envelope diversity, biogenesis and evolution.Nature reviews. Microbiology · 2025Review
- Structural characterization of the POTRA domains from A. baumannii reveals new conformations in BamA.Structure (London, England : 1993) · 2024Article
- Cyclic Isothiocyanate Goitrin ImpairsPlants (Basel, Switzerland) · 2024Article
- Native β-barrel substrates pass through two shared intermediates during folding on the BAM complex.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Dual client binding sites in the ATP-independent chaperone SurA.Nature communications · 2024Article
- The translocation assembly module (TAM) catalyzes the assembly of bacterial outer membrane proteins in vitro.Nature communications · 2024Article
- Discovery and Characterization of Two Folded Intermediates for Outer Membrane Protein TolC Biogenesis.Journal of molecular biology · 2024Article
24 more citing papers are in PubMed but not listed here.
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2 authors.
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Abstract
The integration of β-barrel proteins into the bacterial outer membrane (OM) is catalysed by the β-barrel assembly machinery (BAM). The central BAM subunit (BamA) itself contains a β-barrel domain that is essential for OM protein biogenesis, but its mechanism of action is unknown. To elucidate its function, here we develop a method to trap a native Escherichia coli β-barrel protein bound stably to BamA at a late stage of assembly in vivo. Using disulfide-bond crosslinking, we find that the first β-strand of a laterally 'open' form of the BamA β-barrel forms a rigid interface with the C-terminal β-strand of the substrate. In contrast, the lipid-facing surface of the last two BamA β-strands forms weaker, conformationally heterogeneous interactions with the first β-strand of the substrate that likely represent intermediate assembly states. Based on our results, we propose that BamA promotes the membrane integration of partially folded β-barrels by a 'swing' mechanism.
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