View source for 9jtw


==AtALMT1 with LMNG and sterol mimic CHS==
<StructureSection load='9jtw' size='340' side='right'caption='[[9jtw]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9jtw]] 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=9JTW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9JTW 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]] 3.7&#8491;</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=9jtw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9jtw OCA], [https://pdbe.org/9jtw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9jtw RCSB], [https://www.ebi.ac.uk/pdbsum/9jtw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9jtw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ALMT1_ARATH ALMT1_ARATH] Malate transporter critical for aluminum tolerance. The STOP1 transcription factor is required for ALMT1 expression.<ref>PMID:16740662</ref> <ref>PMID:17885092</ref> <ref>PMID:18826429</ref> <ref>PMID:19321711</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 9jtw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Lee S]]
[[Category: Lee Y]]