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.

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.

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

A structure of the complete, membrane bound, COPII coat solved by sub-tomogram averaging reveals the arrangement of all protein subunits on the membrane and suggests a mechanism for coating heterogeneously-shaped carriers.

Temperature-sensitive mitochondrial outer membrane proteins used as novel quality control substrates reveal a unique mitochondria-associated degradation pathway consisting of both cytosolic and mitochondrial ubiquitin-proteasome system machinery.

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

The crystal structure of a ternary complex of a TonB-dependent transporter containing a signalling domain, bound to siderophore as well as TonB, provides mechanistic insights into siderophore uptake and signalling.

The protein translocation apparatus of the inner- (Sec) and outer-membrane (BAM) interact to form a trans-periplasmic super-complex capable of long-range, PMF-dependent conformational changes to facilitate efficient outer-membrane protein maturation.