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. 2022 Mar 2;8(9):eabm3238. doi: 10.1126/sciadv.abm3238

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Fig. 9. — (A) Model for the GmALMT12/QUAC1 channel regulation. (B) Upon malate binding, GmALMT12/QUAC1 undergoes intramolecular domain reorganization within the twisted two-layer architecture and subsequently induces the conformational change of the toggle switch W90. These changes promote the channel conversion from closed to open state. Other modulations, such as phosphorylation or calmodulin binding, can further enhance the malate-mediated activation, probably via the release of its inhibitory domain-swapped helix from the interprotomer interaction.