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Updated: Apr 3, 2026

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
Published on: July 4, 2016
BamA Alone Accelerates Outer Membrane Protein Folding In Vitro through a Catalytic Mechanism
Ashlee M Plummer1, Karen G Fleming1
1Thomas C. Jenkins Department of Biophysics, Johns Hopkins University , 3400 North Charles Street, Baltimore, Maryland 21218, United States.
Abstract:
β-Barrel assembly machinery protein A (BamA) plays a critical role in the biogenesis of outer membrane proteins (OMPs); however, a mechanistic understanding of its function is lacking. Here, we report an in vitro assay that investigates whether the mechanism of BamA-catalyzed OMP folding is stoichiometric or catalytic. We found that BamA accelerates the folding of OMPs in vitro via a catalytic mechanism, similar to the activity of the full multiprotein β-barrel assembly machinery (BAM) complex in vivo. As BamA alone can repeatedly facilitate the folding of OMPs, we suggest the additional BAM components accelerate this basal activity to biologically relevant time scales.
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