3K3F

Crystal Structure of the Urea Transporter from Desulfovibrio Vulgaris

3K3F の概要

• エントリーDOI: 10.2210/pdb3k3f/pdb
• 関連するPDBエントリー: 3K3G
• 分子名称: Urea transporter, GOLD ION (3 entities in total)
• 機能のキーワード: membrane protein, channel, urea transport, transporter, transport protein, structural genomics, psi-2, protein structure initiative, new york consortium on membrane protein structure, nycomps
• 由来する生物種: Desulfovibrio vulgaris
• 細胞内の位置: Cell membrane ; Multi-pass membrane protein : Q72CX3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37787.19

構造登録者

Levin, E.J.,Zhou, M.,New York Consortium on Membrane Protein Structure (NYCOMPS) (登録日: 2009-10-02, 公開日: 2009-11-17, 最終更新日: 2024-02-21)

主引用文献

Levin, E.J.,Quick, M.,Zhou, M.
Crystal structure of a bacterial homologue of the kidney urea transporter.
Nature, 462:757-761, 2009

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: 19865084
DOI: 10.1038/nature08558

実験手法

X-RAY DIFFRACTION (2.3 Å)