There is a strand-based evolutionary mechanism for the diversification of outer membrane proteins, which has implications for how repeat proteins are created and for how outer membrane proteins fold.

Dispensable loops shield the functionally-important extracellular loops of the essential Gram-negative bacterial outer membrane protein LptD from antibody interference.

Physical contact between two Myxococcus xanthus cells is sufficient to fuse their outer membrane transiently and exchange outer membrane proteins and lipids at high efficiency.

Auxiliary proteins play functional roles in modulating the assembly and activity of a non-canonical ABC transporter that is important for the maintenance of outer membrane lipid asymmetry.

The range of barrel-shaped proteins found in the outer membrane of certain bacteria evolved through multiple pathways.

Input from computational models has enabled the detection of allosteric communication that modulates the gating mechanism of a bacterial outer-membrane protein.

Outer membrane β-barrel proteins in Gram-negative bacteria are assembled within the lumen of the BamA β-barrel.

The pilus extrusion/DNA uptake system of Thermus thermophilus contains a 13-mer of the 757-residue PilQ protein and a tightly bound protein outside the outer membrane with a role in DNA binding.

An actin nucleating protein, Spire1C, localizes to the mitochondrial outer membrane and interacts with the endoplasmic reticulum-anchored formin protein INF2 to drive mitochondrial fission.