7VOJ

Al-bound structure of the AtALMT1 mutant M60A

7VOJ の概要

• エントリーDOI: 10.2210/pdb7voj/pdb
• EMDBエントリー: 32050
• 分子名称: Aluminum-activated malate transporter 1, ACETIC ACID, ALUMINUM ION (3 entities in total)
• 機能のキーワード: almt1, aluminum resistance, malate transport, transport protein
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 113841.27

構造登録者

Wang, J. (登録日: 2021-10-14, 公開日: 2021-12-01, 最終更新日: 2024-06-19)

主引用文献

Wang, J.,Yu, X.,Ding, Z.J.,Zhang, X.,Luo, Y.,Xu, X.,Xie, Y.,Li, X.,Yuan, T.,Zheng, S.J.,Yang, W.,Guo, J.
Structural basis of ALMT1-mediated aluminum resistance in Arabidopsis.
Cell Res., 32:89-98, 2022

PubMed Abstract: The plant aluminum (Al)-activated malate transporter ALMT1 mediates the efflux of malate to chelate the Al in acidic soils and underlies the plant Al resistance. Here we present cryo-electron microscopy (cryo-EM) structures of Arabidopsis thaliana ALMT1 (AtALMT1) in the apo, malate-bound, and Al-bound states at neutral and/or acidic pH at up to 3.0 Å resolution. The AtALMT1 dimer assembles an anion channel and each subunit contains six transmembrane helices (TMs) and six cytosolic α-helices. Two pairs of Arg residues are located in the center of the channel pore and contribute to malate recognition. Al binds at the extracellular side of AtALMT1 and induces conformational changes of the TM1-2 loop and the TM5-6 loop, resulting in the opening of the extracellular gate. These structures, along with electrophysiological measurements, molecular dynamic simulations, and mutagenesis study in Arabidopsis, elucidate the structural basis for Al-activated malate transport by ALMT1.

PubMed: 34799726
DOI: 10.1038/s41422-021-00587-6

実験手法

ELECTRON MICROSCOPY (3 Å)