7W6K

Cryo-EM structure of GmALMT12/QUAC1 anion channel

7W6K の概要

• エントリーDOI: 10.2210/pdb7w6k/pdb
• EMDBエントリー: 32328
• 分子名称: GmALMT12/QUAC1 (1 entity in total)
• 機能のキーワード: symmetrical dimer, t-shaped pore, twisted two-layer architecture, malate-modulation, membrane protein
• 由来する生物種: Glycine max (soybean)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 120643.94

構造登録者

Qin, L.,Tang, L.H.,Xu, J.S.,Zhang, X.H.,Zhu, Y.,Sun, F.,Su, M.,Zhai, Y.J.,Chen, Y.H. (登録日: 2021-12-01, 公開日: 2022-03-16, 最終更新日: 2024-06-26)

主引用文献

Qin, L.,Tang, L.H.,Xu, J.S.,Zhang, X.H.,Zhu, Y.,Zhang, C.R.,Wang, M.H.,Liu, X.L.,Li, F.,Sun, F.,Su, M.,Zhai, Y.,Chen, Y.H.
Cryo-EM structure and electrophysiological characterization of ALMT from Glycine max reveal a previously uncharacterized class of anion channels.
Sci Adv, 8:eabm3238-eabm3238, 2022

PubMed Abstract: Aluminum-activated malate transporters (ALMTs) form an anion channel family that plays essential roles in diverse functions in plants. ALMT12, also named QUAC1 (quick anion channel 1), regulates stomatal closure in response to environmental stimuli. However, the molecular basis of ALMT12/QUAC1 activity remains elusive. Here, we describe the cryo-EM structure of ALMT12/QUAC1 from at 3.5-Å resolution. ALMT12/QUAC1 is a symmetrical dimer, forming a single electropositive T-shaped pore across the membrane. The transmembrane and cytoplasmic domains are assembled into a twisted two-layer architecture, with their associated dimeric interfaces nearly perpendicular. ALMT12/QUAC1-mediated currents display rapid kinetics of activation/deactivation and a bell-shaped voltage dependency, reminiscent of the rapid (R)-type anion currents. Our structural and functional analyses reveal a domain-twisting mechanism for malate-mediated activation. Together, our study uncovers the molecular basis for a previously uncharacterized class of anion channels and provides insights into the gating and modulation of the ALMT12/QUAC1 anion channel.

PubMed: 35235352
DOI: 10.1126/sciadv.abm3238

実験手法

ELECTRON MICROSCOPY (3.5 Å)