To be, or not to be two sites: that is the question about LeuT substrate binding

Nicolas Reyes (1) , Sotiria Tavoulari (2)

1 Weill Medical College of Cornell University [New York]
2 Yale University [New Haven]

Transport proteins of the neurotransmitter sodium symporter (NSS) family regulate the extracellular concentration of several neurotransmitters in the central nervous system. The only member of this family for which atomic-resolution structural data are available is the prokaryotic homologue LeuT. This protein has been used as a model system to study the molecular mechanism of transport of the NSS family. In this Journal Club, we discuss two strikingly different LeuT transport mechanisms: one involving a single high-affinity substrate binding site and one recently proposed alternative involving two high-affinity substrate binding sites that are allosterically coupled.

Domains: Biochemistry, Molecular Biology; Biophysics

Nicolas Reyes, Sotiria Tavoulari. To be, or not to be two sites: that is the question about LeuT substrate binding. Journal of General Physiology, 2011, 138 (4), pp.467 - 471. ⟨10.1085/jgp.201110652⟩. ⟨pasteur-01655623⟩