View source for 7lz2


==Structure of glutamate receptor-like channel GLR3.4 ligand-binding domain in complex with methionine==
<StructureSection load='7lz2' size='340' side='right'caption='[[7lz2]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7lz2]] is a 3 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=7LZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LZ2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=7lz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lz2 OCA], [https://pdbe.org/7lz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lz2 RCSB], [https://www.ebi.ac.uk/pdbsum/7lz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lz2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GLR34_ARATH GLR34_ARATH] Glutamate-gated receptor that probably acts as non-selective cation channel, at least in hypocotyls (Probable). Can be triggered by Asn, Ser, Gly and, to a lower extent, Ala, Cys and Glu (PubMed:18162597, PubMed:22447719). May be involved in light-signal transduction and calcium homeostasis via the regulation of calcium influx into cells (Probable). Plays an important role in the calcium-based fast transmission of environmental stress (PubMed:15864638). Acts as negative regulator of lateral root initiation and development (PubMed:23590882). May restrict primordia numbers and position along the root axis by a signaling process originating in the phloem (PubMed:23590882). AtGLR3.4-mediated cytosolic calcium influx may be involved in the regulation of seed germination under salt stress by modulating sodium accumulation through the SOS pathway (PubMed:29432559).<ref>PMID:15864638</ref> <ref>PMID:18162597</ref> <ref>PMID:22447719</ref> <ref>PMID:23590882</ref> <ref>PMID:29432559</ref> <ref>PMID:15864638</ref> <ref>PMID:21110940</ref> 
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== Publication Abstract from PubMed ==
Glutamate receptor-like channels (GLRs) play vital roles in various physiological processes in plants, such as wound response, stomatal aperture control, seed germination, root development, innate immune response, pollen tube growth, and morphogenesis. Despite the importance of GLRs, knowledge about their molecular organization is limited. Here we use X-ray crystallography and single-particle cryo-EM to solve structures of the Arabidopsis thaliana GLR3.4. Our structures reveal the tetrameric assembly of GLR3.4 subunits into a three-layer domain architecture, reminiscent of animal ionotropic glutamate receptors (iGluRs). However, the non-swapped arrangement between layers of GLR3.4 domains, binding of glutathione through S-glutathionylation of cysteine C205 inside the amino-terminal domain clamshell, unique symmetry, inter-domain interfaces, and ligand specificity distinguish GLR3.4 from representatives of the iGluR family and suggest distinct features of the GLR gating mechanism. Our work elaborates on the principles of GLR architecture and symmetry and provides a molecular template for deciphering GLR-dependent signaling mechanisms in plants.

Structure of the Arabidopsis thaliana glutamate receptor-like channel GLR3.4.,Green MN, Gangwar SP, Michard E, Simon AA, Portes MT, Barbosa-Caro J, Wudick MM, Lizzio MA, Klykov O, Yelshanskaya MV, Feijo JA, Sobolevsky AI Mol Cell. 2021 Jun 17. pii: S1097-2765(21)00409-3. doi:, 10.1016/j.molcel.2021.05.025. PMID:34161757<ref>PMID:34161757</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 7lz2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Gangwar SP]]
[[Category: Green MN]]
[[Category: Sobolevsky AI]]