Structure of MlaFB reveals how a small binding protein and the C-terminal tail on an ATPase subunit work together to regulate the assembly and function of an ABC transporter.

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

Single-turnover studies reveal quantitative insights into the inner mechanics and unfold hidden facets in the conformational coupling of ATP binding, hydrolysis, and substrate translocation by ABC transporters.

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

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

The conformational dynamics of multidrug resistance protein 1 (MRP1) are tracked in real time by single-molecule fluorescence resonance energy transfer experiments, which elucidate the rate-limiting mechanism of MRP1's transport cycle.

By random nonstandard peptide integrated discovery, combinatorial macrocyclic peptides were leavaged that target a heterodimeric ABC transport complex and explore fundamental principles of the substrate translocation cycle.

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

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

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