7lz0: Difference between revisions
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<StructureSection load='7lz0' size='340' side='right'caption='[[7lz0]], [[Resolution|resolution]] 2.29Å' scene=''> | <StructureSection load='7lz0' size='340' side='right'caption='[[7lz0]], [[Resolution|resolution]] 2.29Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'> | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LZ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LZ0 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]] 2.29Å</td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.29Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=7lz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lz0 OCA], [https://pdbe.org/7lz0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lz0 RCSB], [https://www.ebi.ac.uk/pdbsum/7lz0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lz0 ProSAT]</span></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=7lz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lz0 OCA], [https://pdbe.org/7lz0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lz0 RCSB], [https://www.ebi.ac.uk/pdbsum/7lz0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lz0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Gangwar SP]] | [[Category: Gangwar SP]] | ||
[[Category: Green MN]] | [[Category: Green MN]] | ||
[[Category: Sobolevsky AI]] | [[Category: Sobolevsky AI]] | ||
Latest revision as of 11:58, 17 October 2024
Structure of glutamate receptor-like channel GLR3.4 ligand-binding domain in complex with glutamateStructure of glutamate receptor-like channel GLR3.4 ligand-binding domain in complex with glutamate
Structural highlights
Publication Abstract from PubMedGlutamate 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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