3K3G
Crystal Structure of the Urea Transporter from Desulfovibrio Vulgaris Bound to 1,3-dimethylurea
Summary for 3K3G
| Entry DOI | 10.2210/pdb3k3g/pdb |
| Related | 3K3F |
| Descriptor | Urea transporter, GOLD ION, 1,3-dimethylurea, ... (4 entities in total) |
| Functional Keywords | membrane protein, channel, urea transport, transporter, transport protein, structural genomics, psi-2, protein structure initiative, new york consortium on membrane protein structure, nycomps |
| Biological source | Desulfovibrio vulgaris |
| Cellular location | Cell membrane ; Multi-pass membrane protein : Q72CX3 |
| Total number of polymer chains | 1 |
| Total formula weight | 37963.40 |
| Authors | Levin, E.J.,Zhou, M.,New York Consortium on Membrane Protein Structure (NYCOMPS) (deposition date: 2009-10-02, release date: 2009-11-17, Last modification date: 2024-10-16) |
| Primary citation | Levin, E.J.,Quick, M.,Zhou, M. Crystal structure of a bacterial homologue of the kidney urea transporter. Nature, 462:757-761, 2009 Cited by PubMed 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 A 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 alpha-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. PubMed: 19865084DOI: 10.1038/nature08558 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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