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Significance Na+ -coupled symporters use the cellular Na+ gradient to power transport of physiologically important molecules across the lipid membrane. However, the mechanism by which binding and dissociation of Na+ drive transport remains undefined. This work investigated the Na+ /hydantoin transporter Mhp1, a member of the LeuT-fold class of transporters, to describe the conformations sampled during its transport cycle and elucidate the ligand-induced shifts in its conformational equilibrium. The results of this study suggest that Mhp1 isomerization between inward- and outward-facing conformations are Na+ -independent and that coupling to the Na+ gradient occurs through modulation of substrate affinity by Na+ coordination. A previously unidentified model of Mhp1 transport defined by ligand-independent equilibrium fluctuations emerges from this work, offering a new perspective on Na+ -coupled symport in the LeuT-fold.

Conformational cycle and ion-coupling mechanism of the Na + /hydantoin transporter Mhp1

Conformational cycle and ion-coupling mechanism of the Na ⁺ /hydantoin transporter Mhp1