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Updated: Mar 7, 2026

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
Published on: July 4, 2016
The β-barrel assembly machinery in motion
Nicholas Noinaj1, James C Gumbart2, Susan K Buchanan3
1Markey Center for Structural Biology, Department of Biological Sciences and the Purdue Institute for Inflammation, Immunology and Infectious Disease, Purdue University, West Lafayette, Indiana 47907, USA.
Abstract:
In Gram-negative bacteria, the biogenesis of β-barrel outer membrane proteins (OMPs) is mediated by the β-barrel assembly machinery (BAM) complex. During the past decade, structural and functional studies have collectively contributed to advancing our understanding of the structure and function of the BAM complex; however, the exact mechanism that is involved remains elusive. In this Progress article, we discuss recent structural studies that have revealed that the accessory proteins may regulate essential unprecedented conformational changes in the core component BamA during function. We also detail the mechanistic insights that have been gained from structural data, mutagenesis studies and molecular dynamics simulations, and explore two emerging models for the BAM-mediated biogenesis of OMPs in bacteria.
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