Neurotransmitter/sodium symporter orthologue LeuT has a single high-affinity substrate site

Chayne L. Piscitelli, Harini Krishnamurthy and Eric Gouaux ()
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Chayne L. Piscitelli: Oregon Health and Science University
Harini Krishnamurthy: Vollum Institute, Oregon Health and Science University
Eric Gouaux: Vollum Institute, Oregon Health and Science University

Nature, 2010, vol. 468, issue 7327, 1129-1132

Abstract: Crystal structure of LeuT Neurotransmitter sodium-coupled symporters (NSSs) couple the uptake of a neurotransmitter with one or more sodium ions, removing the neurotransmitter from the synaptic cleft. LeuT, a prokaryotic orthologue of the NSS family, has been used to explore the relationship between molecular mechanism and atomic structure in a broad range of transporters. There is some controversy over whether there are one or two high-affinity substrate-binding sites in LeuT. The initial crystal structure of LeuT, together with subsequent functional and structural studies, provided direct evidence for a single, high-affinity substrate-binding site. Recent binding, flux and molecular simulation studies, however, have been interpreted in terms of a model where there are two high-affinity binding sites: the second (S2) site is thought to be located within the extracellular vestibule. In this paper, the authors perform direct measurement of substrate binding to wild-type LeuT and to S2 site mutants using isothermal titration calorimetry, equilibrium dialysis and scintillation proximity assays. The authors conclude that LeuT harbours a single, centrally located, high-affinity substrate-binding site.

Date: 2010
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DOI: 10.1038/nature09581

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