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.

The structural and mechanistic characterization of competitive inhibition of human DMT1 offers a promising route for the development of compounds for the treatment of iron overload disorders.

The structure of the potassium-chloride cotransporter KCC4 provides insight into the basis of ion specificity, transport stoichiometry, and activity regulation for a broadly physiologically and clinically important transporter family.

The cryo-EM structure and functional characterization of the chloride-selective ion transporter Slc26a9 defines its oligomeric architecture and transport mechanism.

Potassium presumably binds to the Na1 site in LeuT, playing a role in inwardly rectifying the transport of substrates.

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.

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

Sodium ions control the rates of both substrate binding and dissociation of an archaeal homologue of glutamate transporters in a manner that minimizes binding intermediates and maximizes transport efficiency.

The inward-open and outward-open structures of MjNhaP1 explain the mechanism of electroneutral sodium-proton antiport across the cell membrane.

A cryo-electron microscopy study of the human CLC-1 chloride ion channel reveals the structural basis of why some CLC proteins function as passive chloride channels whereas others function as an active proton-chloride antiporters.