Dept. of Biochemistry and Molecular Biology
Oregon Health & Science University
The mechanism of ion-coupled secondary transport is universally utilized in every kingdom of life to catalyze the concentrative uptake of molecules across cellular membranes. Ion-coupled transporters are central to many physiological functions ranging from nutrient uptake to neural synaptic transmission. Recently, the crystal structure of the ion-coupled transporter LeuT, a bacterial homolog of the Neurotransmitter:Sodium Symporter (NSS) family, was solved. This structure revealed a novel transporter motif characterized by an internal 2-fold structural repeat, with the substrate L-leucine and two sodium ions bound in a centrally located occluded binding site, suggestive of an alternating access transport mechanism. To date, LeuT presents one of only a small handful of sodium-coupled secondary transporters structures, and remains the only NSS transporter to have yielded to crystallographic studies. LeuT has therefore become widely used as the structural blueprint for modeling and interp
School of Medicine
Piscitelli, Chayne L., "Structure and mechanism of the bacterial transporter LeuT" (2011). Scholar Archive. 666.