3k3f
From Proteopedia
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===Crystal Structure of the Urea Transporter from Desulfovibrio Vulgaris=== | ===Crystal Structure of the Urea Transporter from Desulfovibrio Vulgaris=== | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[3k3f]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K3F OCA]. | |
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| + | ==See Also== | ||
| + | *[[Urea transporter|Urea transporter]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:019865084</ref><references group="xtra"/> |
| - | [[Category: Desulfovibrio vulgaris | + | [[Category: Desulfovibrio vulgaris]] |
[[Category: Levin, E J.]] | [[Category: Levin, E J.]] | ||
[[Category: NYCOMPS, New York Consortium on Membrane Protein Structure.]] | [[Category: NYCOMPS, New York Consortium on Membrane Protein Structure.]] | ||
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[[Category: Transporter]] | [[Category: Transporter]] | ||
[[Category: Urea transport]] | [[Category: Urea transport]] | ||
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Revision as of 10:22, 11 March 2013
Contents |
Crystal Structure of the Urea Transporter from Desulfovibrio Vulgaris
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.
Crystal structure of a bacterial homologue of the kidney urea transporter., Levin EJ, Quick M, Zhou M, Nature. 2009 Dec 10;462(7274):757-61. Epub . PMID:19865084
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
3k3f is a 1 chain structure with sequence from Desulfovibrio vulgaris. Full crystallographic information is available from OCA.
See Also
Reference
- Levin EJ, Quick M, Zhou M. Crystal structure of a bacterial homologue of the kidney urea transporter. Nature. 2009 Dec 10;462(7274):757-61. Epub . PMID:19865084 doi:10.1038/nature08558
Categories: Desulfovibrio vulgaris | Levin, E J. | NYCOMPS, New York Consortium on Membrane Protein Structure. | Zhou, M. | Channel | Membrane protein | New york consortium on membrane protein structure | Nycomp | Protein structure initiative | Psi-2 | Structural genomic | Transport protein | Transporter | Urea transport
