Multiple cryo-electron microscopy structures of a plant ABC transporter exporting glutathione derivatives captured a closed conformation proposed to enforce the export directionality, while a complex central to the coupling mechanism containing both glutathione and closed nucleotide binding domains remains elusive.

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.

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

NmMetQ is a lipoprotein that tethers to membranes via a lipid anchor and has dual function and localization, playing a role in NmMetNI-mediated transport at the inner membrane and moonlighting on the bacterial surface.

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.

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.

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

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.

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.