3k3f

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'''Unreleased structure'''
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[[Image:3k3f.jpg|left|200px]]
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The entry 3k3f is ON HOLD until Paper Publication
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{{STRUCTURE_3k3f| PDB=3k3f | SCENE= }}
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Authors: Levin, E.J., Zhou, M., New York Consortium on Membrane Protein Structure (NYCOMPS)
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===Crystal Structure of the Urea Transporter from Desulfovibrio Vulgaris===
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Description: Crystal Structure of the Urea Transporter from Desulfovibrio Vulgaris
 
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{{ABSTRACT_PUBMED_19865084}}
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==About this Structure==
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3K3F is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris_str._hildenborough Desulfovibrio vulgaris str. hildenborough]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K3F OCA].
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==Reference==
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<ref group="xtra">PMID:19865084</ref><references group="xtra"/>
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[[Category: Desulfovibrio vulgaris str. hildenborough]]
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[[Category: Levin, E J.]]
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[[Category: NYCOMPS, New York Consortium on Membrane Protein Structure.]]
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[[Category: Zhou, M.]]
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[[Category: Channel]]
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[[Category: Membrane protein]]
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[[Category: New york consortium on membrane protein structure]]
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[[Category: Nycomp]]
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[[Category: Protein structure initiative]]
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[[Category: Psi-2]]
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[[Category: Structural genomic]]
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[[Category: Transport protein]]
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[[Category: Transporter]]
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[[Category: Urea transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 18 19:29:00 2009''

Revision as of 17:29, 18 November 2009

Template:STRUCTURE 3k3f

Crystal Structure of the Urea Transporter from Desulfovibrio Vulgaris

Publication Abstract from PubMed

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 of sequence from Desulfovibrio vulgaris str. hildenborough. Full crystallographic information is available from OCA.

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

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