8ZTK

AtALMT9 with LMNG (cis2 class)

8ZTK の概要

• エントリーDOI: 10.2210/pdb8ztk/pdb
• EMDBエントリー: 60465
• 分子名称: Aluminum-activated malate transporter 9, 2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL HEXADECANOATE (3 entities in total)
• 機能のキーワード: plant, stomata, vacuole, almt, ion channel, membrane protein
• 由来する生物種: Arabidopsis thaliana (thale cress)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 135539.80

構造登録者

Lee, Y.,Lee, S. (登録日: 2024-06-07, 公開日: 2025-03-12)

主引用文献

Lee, Y.,Demes-Causse, E.,Yoo, J.,Jang, S.Y.,Jung, S.,Jaslan, J.,Hwang, G.S.,Yoo, J.,De Angeli, A.,Lee, S.
Structural basis for malate-driven, pore lipid-regulated activation of the Arabidopsis vacuolar anion channel ALMT9.
Nat Commun, 16:1817-1817, 2025

PubMed Abstract: In plant cells, ALMTs are key plasma and vacuolar membrane-localized anion channels regulating plant responses to the environment. Vacuolar ALMTs control anion accumulation in plant cells and, in guard cells, they regulate stomata aperture. The activation of vacuolar ALMTs depends on voltage and cytosolic malate, but the underlying molecular mechanisms remain elusive. Here we report the cryo-EM structures of ALMT9 from Arabidopsis thaliana (AtALMT9), a malate-activated vacuolar anion channel, in plugged and unplugged lipid-bound states. In all these states, membrane lipids interact with the ion conduction pathway of AtALMT9. We identify two unplugged states presenting two distinct pore width profiles. Combining structural and functional analysis we identified conserved residues involved in ion conduction and in the pore lipid interaction. Molecular dynamics simulations revealed a peculiar anion conduction mechanism in AtALMT9. We propose a voltage-dependent activation mechanism based on the competition between pore lipids and malate at the cytosolic entrance of the channel.

PubMed: 39979303
DOI: 10.1038/s41467-025-56940-5

実験手法

ELECTRON MICROSCOPY (2.78 Å)