4EZC

Crystal Structure of the UT-B Urea Transporter from Bos Taurus

4EZC の概要

• エントリーDOI: 10.2210/pdb4ezc/pdb
• 分子名称: Urea transporter 1, beta-D-glucopyranose, octyl beta-D-glucopyranoside, ... (5 entities in total)
• 機能のキーワード: membrane protein, channel, urea transport, slc14, structural genomics, psi-biology, new york consortium on membrane protein structure, nycomps, permeation, membrane, transport protein
• 由来する生物種: Bos taurus (bovine,cow,domestic cattle,domestic cow)
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: Q5QF96
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 130131.35

構造登録者

Cao, Y.,Levin, E.J.,Zhou, M.,New York Consortium on Membrane Protein Structure (NYCOMPS) (登録日: 2012-05-02, 公開日: 2012-06-27, 最終更新日: 2024-02-28)

主引用文献

Levin, E.J.,Cao, Y.,Enkavi, G.,Quick, M.,Pan, Y.,Tajkhorshid, E.,Zhou, M.
Structure and permeation mechanism of a mammalian urea transporter.
Proc.Natl.Acad.Sci.USA, 109:11194-11199, 2012

PubMed Abstract: As an adaptation to infrequent access to water, terrestrial mammals produce urine that is hyperosmotic to plasma. To prevent osmotic diuresis by the large quantity of urea generated by protein catabolism, the kidney epithelia contain facilitative urea transporters (UTs) that allow rapid equilibration between the urinary space and the hyperosmotic interstitium. Here we report the first X-ray crystal structure of a mammalian UT, UT-B, at a resolution of 2.36 Å. UT-B is a homotrimer and each protomer contains a urea conduction pore with a narrow selectivity filter. Structural analyses and molecular dynamics simulations showed that the selectivity filter has two urea binding sites separated by an approximately 5.0 kcal/mol energy barrier. Functional studies showed that the rate of urea conduction in UT-B is increased by hypoosmotic stress, and that the site of osmoregulation coincides with the location of the energy barrier.

PubMed: 22733730
DOI: 10.1073/pnas.1207362109

実験手法

X-RAY DIFFRACTION (2.36 Å)