View source for 8zth


==AtALMT9 with LMNG (narrow class)==
<StructureSection load='8zth' size='340' side='right'caption='[[8zth]], [[Resolution|resolution]] 2.63&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8zth]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ZTH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ZTH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.63&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D10:DECANE'>D10</scene>, <scene name='pdbligand=OCT:N-OCTANE'>OCT</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8zth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8zth OCA], [https://pdbe.org/8zth PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8zth RCSB], [https://www.ebi.ac.uk/pdbsum/8zth PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8zth ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ALMT9_ARATH ALMT9_ARATH] Vacuolar malate channel. Has a higher selectivity for malate than for fumarate. Exhibits also a weak chloride conductance.<ref>PMID:18005230</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In 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<ref>PMID:39979303</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8zth" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Lee S]]
[[Category: Lee Y]]