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- W2108161822 abstract "The nucleobase–cation–symport-1 (NCS1) transporters are essential components of salvage pathways for nucleobases and related metabolites. Here, we report the 2.85-angstrom resolution structure of the NCS1 benzyl-hydantoin transporter, Mhp1, from Microbacterium liquefaciens. Mhp1 contains 12 transmembrane helices, 10 of which are arranged in two inverted repeats of five helices. The structures of the outward-facing open and substrate-bound occluded conformations were solved, showing how the outward-facing cavity closes upon binding of substrate. Comparisons with the leucine transporter LeuT Aa and the galactose transporter vSGLT reveal that the outward- and inward-facing cavities are symmetrically arranged on opposite sides of the membrane. The reciprocal opening and closing of these cavities is synchronized by the inverted repeat helices 3 and 8, providing the structural basis of the alternating access model for membrane transport." @default.
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- W2108161822 date "2008-10-31" @default.
- W2108161822 modified "2023-10-18" @default.
- W2108161822 title "Structure and Molecular Mechanism of a Nucleobase–Cation–Symport-1 Family Transporter" @default.
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- W2108161822 doi "https://doi.org/10.1126/science.1164440" @default.
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