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| | <StructureSection load='6r85' size='340' side='right'caption='[[6r85]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='6r85' size='340' side='right'caption='[[6r85]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6r85]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R85 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6R85 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6r85]] is a 2 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=6R85 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6R85 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GLR3.3, At1g42540, T8D8.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6r85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r85 OCA], [http://pdbe.org/6r85 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6r85 RCSB], [http://www.ebi.ac.uk/pdbsum/6r85 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6r85 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=6r85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r85 OCA], [https://pdbe.org/6r85 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6r85 RCSB], [https://www.ebi.ac.uk/pdbsum/6r85 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6r85 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GLR33_ARATH GLR33_ARATH]] Glutamate-gated receptor that probably acts as non-selective cation channel, at least in roots and hypocotyls. Can be triggered by Ala, Asn, Cys, Glu, Gly, Ser and glutathione (a tripeptide consisting of Glu-Gly-Cys). Mediates leaf-to-leaf wound signaling. May be involved in light-signal transduction and calcium homeostasis via the regulation of calcium influx into cells.<ref>PMID:17012403</ref> <ref>PMID:18162597</ref> <ref>PMID:23969459</ref> | + | [https://www.uniprot.org/uniprot/GLR33_ARATH GLR33_ARATH] Glutamate-gated receptor that probably acts as non-selective cation channel, at least in roots and hypocotyls. Can be triggered by Ala, Asn, Cys, Glu, Gly, Ser and glutathione (a tripeptide consisting of Glu-Gly-Cys). Mediates leaf-to-leaf wound signaling. May be involved in light-signal transduction and calcium homeostasis via the regulation of calcium influx into cells.<ref>PMID:17012403</ref> <ref>PMID:18162597</ref> <ref>PMID:23969459</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6r85" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6r85" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Alfieri, A]] | + | [[Category: Alfieri A]] |
| - | [[Category: Costa, A]] | + | [[Category: Costa A]] |
| - | [[Category: Pederzoli, R]] | + | [[Category: Pederzoli R]] |
| - | [[Category: Amino acid-binding]]
| + | |
| - | [[Category: Glutamate receptor-like]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| Structural highlights
Function
GLR33_ARATH Glutamate-gated receptor that probably acts as non-selective cation channel, at least in roots and hypocotyls. Can be triggered by Ala, Asn, Cys, Glu, Gly, Ser and glutathione (a tripeptide consisting of Glu-Gly-Cys). Mediates leaf-to-leaf wound signaling. May be involved in light-signal transduction and calcium homeostasis via the regulation of calcium influx into cells.[1] [2] [3]
Publication Abstract from PubMed
Arabidopsis thaliana glutamate receptor-like (GLR) channels are amino acid-gated ion channels involved in physiological processes including wound signaling, stomatal regulation, and pollen tube growth. Here, fluorescence microscopy and genetics were used to confirm the central role of GLR3.3 in the amino acid-elicited cytosolic Ca(2+) increase in Arabidopsis seedling roots. To elucidate the binding properties of the receptor, we biochemically reconstituted the GLR3.3 ligand-binding domain (LBD) and analyzed its selectivity profile; our binding experiments revealed the LBD preference for l-Glu but also for sulfur-containing amino acids. Furthermore, we solved the crystal structures of the GLR3.3 LBD in complex with 4 different amino acid ligands, providing a rationale for how the LBD binding site evolved to accommodate diverse amino acids, thus laying the grounds for rational mutagenesis. Last, we inspected the structures of LBDs from nonplant species and generated homology models for other GLR isoforms. Our results establish that GLR3.3 is a receptor endowed with a unique amino acid ligand profile and provide a structural framework for engineering this and other GLR isoforms to investigate their physiology.
The structural bases for agonist diversity in an Arabidopsis thaliana glutamate receptor-like channel.,Alfieri A, Doccula FG, Pederzoli R, Grenzi M, Bonza MC, Luoni L, Candeo A, Romano Armada N, Barbiroli A, Valentini G, Schneider TR, Bassi A, Bolognesi M, Nardini M, Costa A Proc Natl Acad Sci U S A. 2019 Dec 23. pii: 1905142117. doi:, 10.1073/pnas.1905142117. PMID:31871183[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Qi Z, Stephens NR, Spalding EP. Calcium entry mediated by GLR3.3, an Arabidopsis glutamate receptor with a broad agonist profile. Plant Physiol. 2006 Nov;142(3):963-71. doi: 10.1104/pp.106.088989. Epub 2006 Sep , 29. PMID:17012403 doi:http://dx.doi.org/10.1104/pp.106.088989
- ↑ 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
- ↑ Mousavi SA, Chauvin A, Pascaud F, Kellenberger S, Farmer EE. GLUTAMATE RECEPTOR-LIKE genes mediate leaf-to-leaf wound signalling. Nature. 2013 Aug 22;500(7463):422-6. doi: 10.1038/nature12478. PMID:23969459 doi:http://dx.doi.org/10.1038/nature12478
- ↑ Alfieri A, Doccula FG, Pederzoli R, Grenzi M, Bonza MC, Luoni L, Candeo A, Romano Armada N, Barbiroli A, Valentini G, Schneider TR, Bassi A, Bolognesi M, Nardini M, Costa A. The structural bases for agonist diversity in an Arabidopsis thaliana glutamate receptor-like channel. Proc Natl Acad Sci U S A. 2019 Dec 23. pii: 1905142117. doi:, 10.1073/pnas.1905142117. PMID:31871183 doi:http://dx.doi.org/10.1073/pnas.1905142117
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