The conformational cycle of an ABC heterodimeric transporter reveals a divergence in the structural mechanism of ABC exporters.

Selective import via bacterial ABC importers is facilitated by a hitherto unrecognized complexity in the conformational dynamics of the substrate-binding proteins.

A heterodimeric exporter exhibits conformational equilibria in the presence of nucleotides, suggesting a unified mechanistic model for the conformational cycle of ABC exporters.

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.

Cryo-EM structure of a peptidase-containing ABC transporter in complex with its protein substrate reveals a mechanism of coupling substrate cleavage to translocation.

Structural and biochemical characterization of the protease domain of an ABC transporter demonstrates the basis for recognition of substrate leader peptides.

An Acinetobacter baumannii ABC transporter likely facilitates transport of glycerophospholipids from the inner to the outer membrane.

ECF-CbrT is a bacterial vitamin B12 transporter that is structurally different from the well-characterized transporter BtuCDF, yet has similar functional properties.

A transport protein enables leaf beetle larvae to take up and store plant toxins and use them as part of their own defense strategy.

Two protein kinases are required to activate auxin efflux transporters from plants.