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7vq4
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The apo-state AtALMT1 structure at pH 7.5(ALMT1apo/pH7.5)== |
| + | <StructureSection load='7vq4' size='340' side='right'caption='[[7vq4]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7vq4]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VQ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VQ4 FirstGlance]. <br> | ||
| + | </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=7vq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vq4 OCA], [https://pdbe.org/7vq4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vq4 RCSB], [https://www.ebi.ac.uk/pdbsum/7vq4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vq4 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 == | ||
| + | The plant aluminum (Al)-activated malate transporter ALMT1 mediates the efflux of malate to chelate the Al in acidic soils and underlies the plant Al resistance. Here we present cryo-electron microscopy (cryo-EM) structures of Arabidopsis thaliana ALMT1 (AtALMT1) in the apo, malate-bound, and Al-bound states at neutral and/or acidic pH at up to 3.0 A resolution. The AtALMT1 dimer assembles an anion channel and each subunit contains six transmembrane helices (TMs) and six cytosolic alpha-helices. Two pairs of Arg residues are located in the center of the channel pore and contribute to malate recognition. Al binds at the extracellular side of AtALMT1 and induces conformational changes of the TM1-2 loop and the TM5-6 loop, resulting in the opening of the extracellular gate. These structures, along with electrophysiological measurements, molecular dynamic simulations, and mutagenesis study in Arabidopsis, elucidate the structural basis for Al-activated malate transport by ALMT1. | ||
| - | + | Structural basis of ALMT1-mediated aluminum resistance in Arabidopsis.,Wang J, Yu X, Ding ZJ, Zhang X, Luo Y, Xu X, Xie Y, Li X, Yuan T, Zheng SJ, Yang W, Guo J Cell Res. 2021 Nov 19. pii: 10.1038/s41422-021-00587-6. doi:, 10.1038/s41422-021-00587-6. PMID:34799726<ref>PMID:34799726</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Wang, J | + | <div class="pdbe-citations 7vq4" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Wang, J Q]] | ||
| + | [[Category: Almt1]] | ||
| + | [[Category: Aluminum resistance]] | ||
| + | [[Category: Malate transport]] | ||
| + | [[Category: Transport protein]] | ||
Current revision
The apo-state AtALMT1 structure at pH 7.5(ALMT1apo/pH7.5)
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