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• W1967156736 abstract "Urea is highly concentrated in the mammalian kidney to produce the osmotic gradient necessary for water re-absorption. Free diffusion of urea across cell membranes is slow owing to its high polarity, and specialized urea transporters have evolved to achieve rapid and selective urea permeation. Here we present the 2.3 Å structure of a functional urea transporter from the bacterium Desulfovibrio vulgaris. The transporter is a homotrimer, and each subunit contains a continuous membrane-spanning pore formed by the two homologous halves of the protein. The pore contains a constricted selectivity filter that can accommodate several dehydrated urea molecules in single file. Backbone and side-chain oxygen atoms provide continuous coordination of urea as it progresses through the filter, and well-placed α-helix dipoles provide further compensation for dehydration energy. These results establish that the urea transporter operates by a channel-like mechanism and reveal the physical and chemical basis of urea selectivity. The osmotic gradient necessary to facilitate water resorption in the kidney is maintained by high concentrations of urea. The free diffusion of urea across the cell membrane is slow, so highly conserved urea transporters have evolved to facilitate selective permeation of urea. Here Levin et al. report the X-ray crystal structure of a bacterial homologue of the urea transporter, from Desulfovibrio vulgaris. The transporter contains a pore with a selectivity filter that can accommodate multiple dehydrated urea molecules in single file, revealing that the transporter operates by a channel-like mechanism. Specialized urea transporters have evolved to achieve rapid and selective urea permeation in the mammalian kidney, a process ultimately necessary for water re-absorption. Here, the X-ray crystal structure of a functional urea transporter from the bacterium Desulfovibrio vulgaris is presented and analysed; the results establish that the urea transporter operates by a channel-like mechanism and reveal the physical and chemical basis of urea selectivity." @default.
• W1967156736 created "2016-06-24" @default.
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• W1967156736 date "2009-10-28" @default.
• W1967156736 modified "2023-10-11" @default.
• W1967156736 title "Crystal structure of a bacterial homologue of the kidney urea transporter" @default.
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• W1967156736 doi "https://doi.org/10.1038/nature08558" @default.
• W1967156736 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2871279" @default.
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