8zte | pdb_00008zte
AtALMT9 with LMNG and sterol mimic CHS (sterol1 class)
Structural highlights
FunctionALMT9_ARATH Vacuolar malate channel. Has a higher selectivity for malate than for fumarate. Exhibits also a weak chloride conductance.[1] Publication Abstract from PubMedIn 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. Structural basis for malate-driven, pore lipid-regulated activation of the Arabidopsis vacuolar anion channel ALMT9.,Lee Y, Demes-Causse E, Yoo J, Jang SY, Jung S, Jaslan J, Hwang GS, Yoo J, De Angeli A, Lee S Nat Commun. 2025 Feb 20;16(1):1817. doi: 10.1038/s41467-025-56940-5. PMID:39979303[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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