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TitleCryo-EM structure and electrophysiological characterization of ALMT from reveal a previously uncharacterized class of anion channels.
Journal, issue, pagesSci Adv, Vol. 8, Issue 9, Page eabm3238, Year 2022
Publish dateMar 4, 2022
AuthorsLi Qin / Ling-Hui Tang / Jia-Shu Xu / Xian-Hui Zhang / Yun Zhu / Chun-Rui Zhang / Mei-Hua Wang / Xue-Lei Liu / Fei Li / Fei Sun / Min Su / Yujia Zhai / Yu-Hang Chen /
PubMed AbstractAluminum-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 ...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.
External linksSci Adv / PubMed:35235352 / PubMed Central
MethodsEM (single particle)
Resolution3.5 Å
Structure data

32328

7w6k

EMDB-32328, PDB-7w6k:
Cryo-EM structure of GmALMT12/QUAC1 anion channel
Method: EM (single particle) / Resolution: 3.5 Å

Source
  • glycine max (soybean)
KeywordsMEMBRANE PROTEIN / Symmetrical dimer / T-shaped pore / twisted two-layer architecture / Malate-modulation

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