Nramp-family transporters adapt a common fold to a novel mechanism in which the spatial and temporal separation of like-charge transition metal and proton co-substrates circumvents the expected electrostatic repulsion.

An ECF-type transporter serves as broad-spectrum heme iron scavenger and allows an opportunistic pathogen to use multiple eukaryotic hemoproteins to overcome nutritional iron-limitation.

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

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.

Phylogenetic and biochemical analyses reveals a shared evolutionary path between biosynthesis and transport of defense metabolites in plants.

Crystal structures of an archaeal homologue of mammalian glutamate transporters in apo and ion-only bound outward- and inward-facing states reveal ion-coupled conformational changes supporting mechanisms of coupling, gating, and transport.

To avoid internal traffic jams of nutrients that they absorb, plants need to swiftly regulate the transporters that take up those nutrients.

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

It is technically difficult to identify transport proteins, but here a method is presented that exploits the principle that they are stabilized in detergent solution when they bind their substrate.

Combined cutting-edge technologies discovered a pair of carboxylate transporters that appears evolutionarily different among novel transporters and that is essential for parasite physiology.