ArticleNature microbiology2025
Structure of a distinct β-barrel assembly machinery complex in the Bacteroidota.
Article in Nature microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- BamA as a next-generation antibacterial target: mechanistic insights, inhibitor landscape, and rational drug design strategies.RSC advances · 2026Review
- A standardized toolkit for programmable protein secretion and surface display inbioRxiv : the preprint server for biology · 2026Article
- Integration of Membrane Proteins into the Outer Membrane of Diderm Bacteria by the BAM Complex.Chemical reviews · 2026Review
- Identification and characterization of the functional LolB ortholog inbioRxiv : the preprint server for biology · 2026Article
- Discovery and characterization of an anti-Frontiers in microbiology · 2026Article
- Bam complex redefined in Bacteroidota.Nature microbiology · 2025Article
- Article
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Authors and funding
11 authors.
Funding
Abstract
The Gram-negative β-barrel assembly machinery (BAM) complex catalyses the folding and membrane insertion of newly synthesized β-barrel outer membrane proteins. The BAM is structurally conserved, but most studies have focused on Gammaproteobacteria. Here, using single-particle cryogenic electron microscopy, quantitative proteomics and functional assays, we show that the BAM complex is distinct within the Bacteroidota. Cryogenic electron microscopy structures of BAM complexes from the human gut symbiont Bacteroides thetaiotaomicron (3.3 Å) and the human oral pathogen Porphyromonas gingivalis (3.2 Å) show similar, seven-component complexes of ~325 kDa. The complexes are mostly extracellular and comprise canonical BamA and BamD; an integral, essential outer membrane protein, BamG, that associates with BamA; and four surface-exposed lipoproteins: BamH-K. Absent from the BAM in Pseudomonadota, BamG-K form a large, extracellular dome that may confer additional functionality to enable the folding and assembly of β-barrel-surface-exposed lipoprotein complexes that are a hallmark of the Bacteroidota. Our findings develop our understanding of fundamental biological processes in an important bacterial phylum.
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