2W1P

1.4 Angstrom crystal structure of P.pastoris aquaporin, Aqy1, in a closed conformation at pH 8.0

2W1P の概要

• エントリーDOI: 10.2210/pdb2w1p/pdb
• 関連するPDBエントリー: 2W2E
• 分子名称: AQUAPORIN PIP2-7 7;, octyl beta-D-glucopyranoside, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: membrane protein, gating, yeast
• 由来する生物種: KOMAGATAELLA PASTORIS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31172.82

構造登録者

Fischer, G.,Kosinska-Eriksson, U.,Aponte-Santamaria, C.,Palmgren, M.,Geijer, C.,Hedfalk, K.,Hohmann, S.,de Groot, B.L.,Neutze, R.,Lindkvist-Petersson, K. (登録日: 2008-10-20, 公開日: 2009-06-16, 最終更新日: 2023-12-13)

主引用文献

Fischer, G.,Kosinska-Eriksson, U.,Aponte-Santamaria, C.,Palmgren, M.,Geijer, C.,Hedfalk, K.,Hohmann, S.,De Groot, B.L.,Neutze, R.,Lindkvist-Petersson, K.
Crystal Structure of a Yeast Aquaporin at 1.15 A Reveals a Novel Gating Mechanism
Plos Biol., 7:130-, 2009

PubMed Abstract: Aquaporins are transmembrane proteins that facilitate the flow of water through cellular membranes. An unusual characteristic of yeast aquaporins is that they frequently contain an extended N terminus of unknown function. Here we present the X-ray structure of the yeast aquaporin Aqy1 from Pichia pastoris at 1.15 A resolution. Our crystal structure reveals that the water channel is closed by the N terminus, which arranges as a tightly wound helical bundle, with Tyr31 forming H-bond interactions to a water molecule within the pore and thereby occluding the channel entrance. Nevertheless, functional assays show that Aqy1 has appreciable water transport activity that aids survival during rapid freezing of P. pastoris. These findings establish that Aqy1 is a gated water channel. Mutational studies in combination with molecular dynamics simulations imply that gating may be regulated by a combination of phosphorylation and mechanosensitivity.

PubMed: 19529756
DOI: 10.1371/JOURNAL.PBIO.1000130

実験手法

X-RAY DIFFRACTION (1.4 Å)