Cryo-EM structure and electrophysiological characterization of ALMT from Glycine max reveal a previously uncharacterized class of anion channels.

The article offers information on the Aluminum-activated malate transporters (ALMTs) form an anion channel family that plays essential roles in diverse functions in plants. It discusses that the molecular basis of ALMT12/QUAC1 activity remains elusive. Here, we describe the cryo-EM structure of ALMT12/QUAC1 from Glycine max at 3.5-Å resolution; and mentions that The transmembrane and cytoplasmic domains are assembled into a twisted two-layer architecture.