Structures of folding intermediates on BAM show diverse substrates fold by a uniform mechanism
Thomson, B. D.; Marquez, M. D.; Rawson, S.; dos Santos, T. M. A.; Harrison, S. C.; Kahne, D.
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The outer membranes of mitochondria, chloroplasts, and Gram-negative bacteria contain {beta}-barrel membrane proteins that are assembled by conserved multi-subunit machines. In bacteria, the {beta}-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.
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