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5I32

Ammonia permeable aquaporin AtTIP2;1

5I32 の概要
エントリーDOI10.2210/pdb5i32/pdb
分子名称Aquaporin TIP2-1 (2 entities in total)
機能のキーワードaquaporin, mip, ammonia-permeable, membrane protein
由来する生物種Arabidopsis thaliana (Mouse-ear cress)
細胞内の位置Vacuole membrane ; Multi-pass membrane protein : Q41951
タンパク質・核酸の鎖数1
化学式量合計28043.02
構造登録者
Kirscht, A.,Nissen, P.,Kjellbom, P.,Gourdon, P.,Johanson, U. (登録日: 2016-02-09, 公開日: 2016-04-06, 最終更新日: 2024-01-10)
主引用文献Kirscht, A.,Kaptan, S.S.,Bienert, G.P.,Chaumont, F.,Nissen, P.,de Groot, B.L.,Kjellbom, P.,Gourdon, P.,Johanson, U.
Crystal Structure of an Ammonia-Permeable Aquaporin.
Plos Biol., 14:e1002411-e1002411, 2016
Cited by
PubMed Abstract: Aquaporins of the TIP subfamily (Tonoplast Intrinsic Proteins) have been suggested to facilitate permeation of water and ammonia across the vacuolar membrane of plants, allowing the vacuole to efficiently sequester ammonium ions and counteract cytosolic fluctuations of ammonia. Here, we report the structure determined at 1.18 Å resolution from twinned crystals of Arabidopsis thaliana aquaporin AtTIP2;1 and confirm water and ammonia permeability of the purified protein reconstituted in proteoliposomes as further substantiated by molecular dynamics simulations. The structure of AtTIP2;1 reveals an extended selectivity filter with the conserved arginine of the filter adopting a unique unpredicted position. The relatively wide pore and the polar nature of the selectivity filter clarify the ammonia permeability. By mutational studies, we show that the identified determinants in the extended selectivity filter region are sufficient to convert a strictly water-specific human aquaporin into an AtTIP2;1-like ammonia channel. A flexible histidine and a novel water-filled side pore are speculated to deprotonate ammonium ions, thereby possibly increasing permeation of ammonia. The molecular understanding of how aquaporins facilitate ammonia flux across membranes could potentially be used to modulate ammonia losses over the plasma membrane to the atmosphere, e.g., during photorespiration, and thereby to modify the nitrogen use efficiency of plants.
PubMed: 27028365
DOI: 10.1371/journal.pbio.1002411
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.18 Å)
構造検証レポート
Validation report summary of 5i32
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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