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Updated: Feb 11, 2026

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
Published on: July 4, 2016
Bacterial machineries for the assembly of membrane-embedded β-barrel proteins
David Ranava1, Anne Caumont-Sarcos1, Cécile Albenne1
1Laboratoire de Microbiologie et de Génétique Moléculaires, Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPS, 118 route de Narbonne, 31062 Toulouse, France.
Abstract:
The outer membrane (OM) of Gram-negative bacteria is an essential organelle that protects cells from external aggressions and mediates the secretion of virulence factors. Efficient assembly of integral OM β-barrel proteins (OMPs) is crucial for the correct functioning of the OM. Biogenesis of OMPs occurs in a stepwise manner that is finalized by the β-barrel assembly machinery (BAM complex). Some OMPs further require the translocation and assembly module (TAM) for efficient and correct integration into the OM. Both the BAM complex and the TAM contain a protein of the Omp85 superfamily and distinct interacting factors. Their mechanism of action, however, remains largely elusive. We summarize and discuss recent structural and biochemical analyses that are helping to elucidate the molecular pathways of OMP assembly.
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