Structure of MlaFEDB ABC transporter with substrate bound in the outward-open pocket of MlaE provides mechanistic insights into lipid transport within the Gram-negative bacterial cell envelope.

In the bacterial small multidrug transporter EmrE, sidechain rearrangements in the binding site accommodate structurally diverse substrates without major rearrangements of the protein backbone.

Serum amyloid A proteins bind retinol with nanomolar affinity, and do so by forming oligomers that create a hydrophobic pocket that shields retinol from the aqueous environment.

Discovery of the structural basis for recognition and uptake of a human precursor for body odour production reveals an important role for bacterial peptide transport and novel routes to prevent its production in humans.

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.

Mechanochemical coupling between interfacial force and biosurfactant kinetics can coordinate large-scale material transport in primitive life forms, suggesting a new principle to engineer self-organized microbial communities.

A combination of bioinformatics, protein biochemistry, and X-ray crystal structures reveals new bacterial proteins that are capable of binding to sterols.

A method for determining how many ions are required to drive transport in an electrogenic secondary active transporter will help understand the mechanisms of bacterial transporters whose structures have been solved.

The conserved polypeptide transport associated (POTRA) domains of the protein import channel, Toc75, are essential for protein import into chloroplasts.

Two thermodynamically distinct transport mechanisms operating within the same binding site explains the remarkable promiscuity of POT family transporters towards peptide and drug ligands.