The C-terminal tail acts as a secondary gate to regulate substrate access into the primary binding site for transport across the membrane.

Studies of the substrate selectivity of concentrative nucleoside transporters provide proof of principle for structure-based improvement of drug delivery by these transporters.

The tripartite drug efflux pump AcrA-AcrB-TolC, representative of a wide group of pumps from Gram-negative bacteria, enters a transport-competent state through long-distance conformational changes that switch the channel from a closed to an open state.

A transport mechanism is uncovered in the major drug-efflux system in E. coli involving two remote alternating-access conformational cycles, which could provide the basis for the development of allosteric inhibitors against multidrug resistance.

Study of TbAQP2 adaptations and substrate interactions shows how this aquaglyceroporin enables cellular entry of large antimicrobial agents in Trypanosoma brucei.

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

The high-resolution x-ray structure of an asymmetrical SeCitS dimer, present in the inward- and outward-facing state, provides a complete mechanism of substrate and ion translocation in a sodium-dependent symporter.

High-performance computing simulations reveal how two remote sites in the multidrug transporter AcrB work together for drug extrusion using the proton-motive force.

Stramenopiles are unusual, because the pay-off phase of glycolysis occurs in mitochondria rather than the cytosol and the identified mitochondrial carrier links the two parts by transporting glycolytic intermediates.

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