7lz0

From Proteopedia

(Difference between revisions)

Revision as of 06:20, 18 August 2021

Structure of glutamate receptor-like channel GLR3.4 ligand-binding domain in complex with glutamate

Structural highlights

7lz0 is a 3 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Gene:	GLR3.4, GLR4, GLUR3, At1g05200, YUP8H12.19 (ARATH)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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).^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

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^[8]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Meyerhoff O, Muller K, Roelfsema MR, Latz A, Lacombe B, Hedrich R, Dietrich P, Becker D. AtGLR3.4, a glutamate receptor channel-like gene is sensitive to touch and cold. Planta. 2005 Oct;222(3):418-27. doi: 10.1007/s00425-005-1551-3. Epub 2005 Apr 28. PMID:15864638 doi:http://dx.doi.org/10.1007/s00425-005-1551-3
↑ Stephens NR, Qi Z, Spalding EP. Glutamate receptor subtypes evidenced by differences in desensitization and dependence on the GLR3.3 and GLR3.4 genes. Plant Physiol. 2008 Feb;146(2):529-38. doi: 10.1104/pp.107.108134. Epub 2007 Dec , 27. PMID:18162597 doi:http://dx.doi.org/10.1104/pp.107.108134
↑ Vincill ED, Bieck AM, Spalding EP. Ca(2+) conduction by an amino acid-gated ion channel related to glutamate receptors. Plant Physiol. 2012 May;159(1):40-6. doi: 10.1104/pp.112.197509. Epub 2012 Mar, 23. PMID:22447719 doi:http://dx.doi.org/10.1104/pp.112.197509
↑ Vincill ED, Clarin AE, Molenda JN, Spalding EP. Interacting glutamate receptor-like proteins in Phloem regulate lateral root initiation in Arabidopsis. Plant Cell. 2013 Apr;25(4):1304-13. doi: 10.1105/tpc.113.110668. Epub 2013 Apr, 16. PMID:23590882 doi:http://dx.doi.org/10.1105/tpc.113.110668
↑ Cheng Y, Zhang X, Sun T, Tian Q, Zhang WH. Glutamate Receptor Homolog3.4 is Involved in Regulation of Seed Germination Under Salt Stress in Arabidopsis. Plant Cell Physiol. 2018 May 1;59(5):978-988. doi: 10.1093/pcp/pcy034. PMID:29432559 doi:http://dx.doi.org/10.1093/pcp/pcy034
↑ Meyerhoff O, Muller K, Roelfsema MR, Latz A, Lacombe B, Hedrich R, Dietrich P, Becker D. AtGLR3.4, a glutamate receptor channel-like gene is sensitive to touch and cold. Planta. 2005 Oct;222(3):418-27. doi: 10.1007/s00425-005-1551-3. Epub 2005 Apr 28. PMID:15864638 doi:http://dx.doi.org/10.1007/s00425-005-1551-3
↑ Teardo E, Formentin E, Segalla A, Giacometti GM, Marin O, Zanetti M, Lo Schiavo F, Zoratti M, Szabo I. Dual localization of plant glutamate receptor AtGLR3.4 to plastids and plasmamembrane. Biochim Biophys Acta. 2011 Mar;1807(3):359-67. doi: 10.1016/j.bbabio.2010.11.008., Epub 2010 Nov 23. PMID:21110940 doi:http://dx.doi.org/10.1016/j.bbabio.2010.11.008
↑ 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. Structure of the Arabidopsis thaliana glutamate receptor-like channel GLR3.4. Mol Cell. 2021 Jun 17. pii: S1097-2765(21)00409-3. doi:, 10.1016/j.molcel.2021.05.025. PMID:34161757 doi:http://dx.doi.org/10.1016/j.molcel.2021.05.025

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7lz0"

@@ Line 1: / Line 1: @@
 ==Structure of glutamate receptor-like channel GLR3.4 ligand-binding domain in complex with glutamate==
-<StructureSection load='7lz0' size='340' side='right'caption='[[7lz0]]' scene=''>
+<StructureSection load='7lz0' size='340' side='right'caption='[[7lz0]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
 == Structural highlights ==
-<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>
+<table><tr><td colspan='2'>[[7lz0]] is a 3 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=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='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>
+</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='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=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>
+== 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.
+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>
+</div>
+<div class="pdbe-citations 7lz0" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
+[[Category: Arath]]
 [[Category: Large Structures]]
-[[Category: Gangwar SP]]
+[[Category: Gangwar, S P]]
-[[Category: Green MN]]
+[[Category: Green, M N]]
-[[Category: Sobolevsky AI]]
+[[Category: Sobolevsky, A I]]
+[[Category: Arabidopsis thaliana]]
+[[Category: Ion-channel]]
+[[Category: Ligand binding domain]]
+[[Category: Membrane protein]]

7lz0

From Proteopedia

Revision as of 06:20, 18 August 2021

Structure of glutamate receptor-like channel GLR3.4 ligand-binding domain in complex with glutamate

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox