2ZZ9

Structure of aquaporin-4 S180D mutant at 2.8 A resolution by electron crystallography

2ZZ9 の概要

• エントリーDOI: 10.2210/pdb2zz9/pdb
• 関連するPDBエントリー: 2D57
• 分子名称: Aquaporin-4, 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (3 entities in total)
• 機能のキーワード: water transport, water channel, aquaporin, two-dimensional crystal, membrane protein, baculovirus expression system, glycoprotein, membrane, phosphoprotein, transmembrane, transport, transport protein
• 由来する生物種: Rattus norvegicus (Rat)
• 細胞内の位置: Membrane; Multi-pass membrane protein: P47863
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35937.56

構造登録者

Tani, K.,Mitsuma, T.,Hiroaki, Y.,Kamegawa, A.,Nishikawa, K.,Tanimura, Y.,Fujiyoshi, Y. (登録日: 2009-02-06, 公開日: 2009-06-09, 最終更新日: 2023-11-08)

主引用文献

Tani, K.,Mitsuma, T.,Hiroaki, Y.,Kamegawa, A.,Nishikawa, K.,Tanimura, Y.,Fujiyoshi, Y.
Mechanism of Aquaporin-4's Fast and Highly Selective Water Conduction and Proton Exclusion.
J.Mol.Biol., 389:694-706, 2009

PubMed Abstract: Members of the aquaporin (AQP) family are expressed in almost every organism, including 13 homologues in humans. Based on the electron crystallographic structure of AQP1, the hydrogen-bond isolation mechanism was proposed to explain why AQPs are impermeable to protons despite their very fast water conduction. The mechanism by which AQPs exclude protons remained controversial, however. Here we present the structure of AQP4 at 2.8 A resolution obtained by electron crystallography of double-layered two-dimensional crystals. The resolution has been improved from the previous 3.2 A, with accompanying improvement in data quality resulting in the ability to identify individual water molecules. Our structure of AQP4, the predominant water channel in the brain, reveals eight water molecules in the channel. The arrangement of the waters provides support for the hydrogen-bond isolation mechanism. Our AQP4 structure also visualizes five lipids, showing that direct interactions of the extracellular surface of AQP4 with three lipids in the adjoining membrane help stabilize the membrane junction.

PubMed: 19406128
DOI: 10.1016/j.jmb.2009.04.049

実験手法

ELECTRON CRYSTALLOGRAPHY (2.8 Å)