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| Title | Structures of folding intermediates on BAM show diverse substrates fold by a uniform mechanism. |
|---|---|
| Journal, issue, pages | bioRxiv, Year 2025 |
| Publish date | Oct 17, 2025 |
 Authors | Benjamin D Thomson / Melissa D Marquez / Shaun Rawson / Thiago M A Dos Santos / Stephen C Harrison / Daniel Kahne |
| PubMed Abstract | The outer membranes of mitochondria, chloroplasts, and Gram-negative bacteria contain β-barrel membrane proteins that are assembled by conserved multi-subunit machines. In bacteria, the β-barrel ...The outer membranes of mitochondria, chloroplasts, and Gram-negative bacteria contain β-barrel membrane proteins that are assembled by conserved multi-subunit machines. In bacteria, the β-barrel assembly machine (BAM) folds over a hundred compositionally different substrates into barrels that vary greatly in size. Some larger barrels require globular proteins to plug the barrel lumen. How a single machine can assemble such different barrels is unknown. Here we report three structures representing progressively folded stages of a 16-stranded barrel engaged with BAM, as well as the structure of a late-stage folding intermediate of a 26-stranded substrate folding around its soluble lipoprotein plug on BAM. We find that BAM catalyzes folding of these substrates by a uniform mechanism in which BAM undergoes major distortions to accommodate the nascent barrel. |
 External links | bioRxiv / PubMed:41280068 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.3 - 3.9 Å |
| Structure data |  EMDB-48251: Consensus refinement of the barrel region of beta-barrel assembly machine from Escherichia coli in an late state of substrate assembly EMDB-48253, PDB-9mge: EMDB-48254, PDB-9mgf: EMDB-48255, PDB-9mgg: |
| Source |
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 Keywords | MEMBRANE PROTEIN / beta-barrel assembly machine / outer membrane / folding intermediate |
escherichia coli k-12 (bacteria)