7lzh: Difference between revisions

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-'''Unreleased structure'''
-The entry 7lzh is ON HOLD
+==Structure of the glutamate receptor-like channel AtGLR3.4==
+<StructureSection load='7lzh' size='340' side='right'caption='[[7lzh]], [[Resolution|resolution]] 3.57&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7lzh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LZH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LZH FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GLR3.4, GLR4, GLUR3, At1g05200, YUP8H12.19 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=7lzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lzh OCA], [https://pdbe.org/7lzh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lzh RCSB], [https://www.ebi.ac.uk/pdbsum/7lzh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lzh 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>
+<div style="background-color:#fffaf0;">
+== 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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 7lzh" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Arath]]
+[[Category: Large Structures]]
+[[Category: Gangwar, S P]]
+[[Category: Green, M N]]
+[[Category: Sobolevsky, A I]]
+[[Category: Arabidopsis thaliana]]
+[[Category: Ion-channel]]
+[[Category: Transport protein]]