2B6O

Electron crystallographic structure of lens Aquaporin-0 (AQP0) (lens MIP) at 1.9A resolution, in a closed pore state

2B6O の概要

• エントリーDOI: 10.2210/pdb2b6o/pdb
• 関連するPDBエントリー: 1SOR 1YMG 2B6P
• 分子名称: Lens fiber major intrinsic protein, 1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE (3 entities in total)
• 機能のキーワード: aquaporin-0 junctions, aqp0, lens mip, lipid-protein interactions, membrane, lipid bilayer, closed water pore, membrane protein
• 由来する生物種: Ovis aries (sheep)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34386.28

構造登録者

Gonen, T.,Cheng, Y.,Sliz, P.,Hiroaki, Y.,Fujiyoshi, Y.,Harrison, S.C.,Walz, T. (登録日: 2005-10-03, 公開日: 2005-12-06, 最終更新日: 2023-08-23)

主引用文献

Gonen, T.,Cheng, Y.,Sliz, P.,Hiroaki, Y.,Fujiyoshi, Y.,Harrison, S.C.,Walz, T.
Lipid-protein interactions in double-layered two-dimensional AQP0 crystals.
Nature, 438:633-638, 2005

PubMed Abstract: Lens-specific aquaporin-0 (AQP0) functions as a specific water pore and forms the thin junctions between fibre cells. Here we describe a 1.9 A resolution structure of junctional AQP0, determined by electron crystallography of double-layered two-dimensional crystals. Comparison of junctional and non-junctional AQP0 structures shows that junction formation depends on a conformational switch in an extracellular loop, which may result from cleavage of the cytoplasmic amino and carboxy termini. In the centre of the water pathway, the closed pore in junctional AQP0 retains only three water molecules, which are too widely spaced to form hydrogen bonds with each other. Packing interactions between AQP0 tetramers in the crystalline array are mediated by lipid molecules, which assume preferred conformations. We were therefore able to build an atomic model for the lipid bilayer surrounding the AQP0 tetramers, and we describe lipid-protein interactions.

PubMed: 16319884
DOI: 10.1038/nature04321

実験手法

ELECTRON CRYSTALLOGRAPHY (1.9 Å)