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• W2046394498 startingPage "14752" @default.
• W2046394498 abstract "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." @default.
• W2046394498 created "2016-06-24" @default.
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• W2046394498 date "2014-09-29" @default.
• W2046394498 modified "2023-10-16" @default.
• W2046394498 title "Conformational cycle and ion-coupling mechanism of the Na ⁺ /hydantoin transporter Mhp1" @default.
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• W2046394498 doi "https://doi.org/10.1073/pnas.1410431111" @default.
• W2046394498 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4205665" @default.
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• W2046394498 hasPublicationYear "2014" @default.
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