The cell envelope of Gram-negative bacteria is a three-layered structure that supports colonisation in harsh environments. The outer membrane (OM) forms the exterior layer of the envelope and is an asymmetric lipid membrane. Interspersed within the lipid membrane are β-barrel proteins that allow both active and passive diffusion of nutrients into cells. These outer membrane proteins (OMPs) are organised in clusters, within protein rich regions known as OMP islands. The organisation and physiological ramifications of OMP islands is currently unknown. To investigate the molecular details of OMP clusters we apply in vivo crosslinking methods, to trap and isolate OMPs in their native membrane environment. Using a combination of mass spectrometry-based methods and cryo-EM, we have uncovered one of the basic architectural units of OMP islands. Although the OM is impervious to many antibiotics such as vancomycin, protein antibiotics known as bacteriocins are able to translocate through this layer, to deliver a potent cytotoxic domain into the cell. Bacteriocins are released by bacterial populations during times of competition for resources. In order to be imported, bacteriocins hijack OMPs, often mimicking natural ligand binding modes. Import of bacteriocins across the OM is underpinned by a translocon complex, comprising an OM receptor and a translocator protein, which together allow the bound toxin to contact one of two energised inner membrane complexes, Tol or Ton, that drive import. Here, we trap and isolate an OM bacteriocin translocon and solve its structure by cryo-EM. Remarkably, the structure reveals that protein bacteriocins exploit the basic architectural unit of OMP islands to form their translocons. This talk will summarise the advances in our understanding of the molecular details of OMP island formation and how this is the basis for bacteriocin import.