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- W4313311955 abstract "Folate (vitamin B9) is the coenzyme involved in one-carbon transfer biochemical reactions essential for cell survival and proliferation, with its inadequacy causing developmental defects or severe diseases. Notably, mammalian cells lack the ability to de novo synthesize folate but instead rely on its intake from extracellular sources via specific transporters or receptors, among which SLC19A1 is the ubiquitously expressed one in tissues. However, the mechanism of substrate recognition by SLC19A1 remains unclear. Here we report the cryo-EM structures of human SLC19A1 and its complex with 5-methyltetrahydrofolate at 3.5-3.6 Å resolution and elucidate the critical residues for substrate recognition. In particular, we reveal that two variant residues among SLC19 subfamily members designate the specificity for folate. Moreover, we identify intracellular thiamine pyrophosphate as the favorite coupled substrate for folate transport by SLC19A1. Together, this work establishes the molecular basis of substrate recognition by this central folate transporter." @default.
- W4313311955 created "2023-01-06" @default.
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- W4313311955 date "2022-12-28" @default.
- W4313311955 modified "2023-10-09" @default.
- W4313311955 title "Molecular mechanism of substrate recognition by folate transporter SLC19A1" @default.
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- W4313311955 doi "https://doi.org/10.1038/s41421-022-00508-w" @default.
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