6s6q
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='6s6q' size='340' side='right'caption='[[6s6q]], [[Resolution|resolution]] 2.95Å' scene=''> | <StructureSection load='6s6q' size='340' side='right'caption='[[6s6q]], [[Resolution|resolution]] 2.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6s6q]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S6Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6S6Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6s6q]] is a 4 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=6S6Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6S6Q FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TYS:O-SULFO-L-TYROSINE'>TYS</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TYS:O-SULFO-L-TYROSINE'>TYS</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GSO1, SGN3, At4g20140, F1C12.60 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></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=6s6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s6q OCA], [http://pdbe.org/6s6q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s6q RCSB], [http://www.ebi.ac.uk/pdbsum/6s6q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s6q ProSAT]</span></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=6s6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s6q OCA], [http://pdbe.org/6s6q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s6q RCSB], [http://www.ebi.ac.uk/pdbsum/6s6q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s6q ProSAT]</span></td></tr> | ||
| Line 11: | Line 12: | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/GSO1_ARATH GSO1_ARATH]] Together with GSO2, receptor-like serine/threonine-kinase required during the development of the epidermal surface in embryos and cotyledons (PubMed:18088309). In coordination with GSO2, regulates root growth through control of cell division and cell fate specification. Controls seedling root growth by modulating sucrose response after germination (PubMed:24123341). Receptor of the peptide hormones CIF1 and CIF2 required for contiguous Casparian strip diffusion barrier formation in roots (PubMed:28104889). Required for localizing CASP proteins into the Casparian strip following an uninterrupted, ring-like domain, to trigger endodermal differentiation and thus regulate potassium ion (K) homeostasis. Involved in the maintenance of water transport and root pressure. May also be involved in the regulation of suberin accumulation in the endodermis (PubMed:25233277).<ref>PMID:18088309</ref> <ref>PMID:24123341</ref> <ref>PMID:25233277</ref> <ref>PMID:28104889</ref> [[http://www.uniprot.org/uniprot/CIF2_ARATH CIF2_ARATH]] Peptide hormone required for contiguous Casparian strip diffusion barrier formation in roots via the regulation of CASPs protein expression and distribution in a GSO1-GSO2 signaling pathway. The Casparian strip is required for ion homeostasis (e.g. iron and potassium ions).<ref>PMID:28104889</ref> | [[http://www.uniprot.org/uniprot/GSO1_ARATH GSO1_ARATH]] Together with GSO2, receptor-like serine/threonine-kinase required during the development of the epidermal surface in embryos and cotyledons (PubMed:18088309). In coordination with GSO2, regulates root growth through control of cell division and cell fate specification. Controls seedling root growth by modulating sucrose response after germination (PubMed:24123341). Receptor of the peptide hormones CIF1 and CIF2 required for contiguous Casparian strip diffusion barrier formation in roots (PubMed:28104889). Required for localizing CASP proteins into the Casparian strip following an uninterrupted, ring-like domain, to trigger endodermal differentiation and thus regulate potassium ion (K) homeostasis. Involved in the maintenance of water transport and root pressure. May also be involved in the regulation of suberin accumulation in the endodermis (PubMed:25233277).<ref>PMID:18088309</ref> <ref>PMID:24123341</ref> <ref>PMID:25233277</ref> <ref>PMID:28104889</ref> [[http://www.uniprot.org/uniprot/CIF2_ARATH CIF2_ARATH]] Peptide hormone required for contiguous Casparian strip diffusion barrier formation in roots via the regulation of CASPs protein expression and distribution in a GSO1-GSO2 signaling pathway. The Casparian strip is required for ion homeostasis (e.g. iron and potassium ions).<ref>PMID:28104889</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Plants use leucine-rich repeat receptor kinases (LRR-RKs) to sense sequence diverse peptide hormones at the cell surface. A 3.0-A crystal structure of the LRR-RK GSO1/SGN3 regulating Casparian strip formation in the endodermis reveals a large spiral-shaped ectodomain. The domain provides a binding platform for 21 amino acid CIF peptide ligands, which are tyrosine sulfated by the tyrosylprotein sulfotransferase TPST/SGN2. GSO1/SGN3 harbors a binding pocket for sulfotyrosine and makes extended backbone interactions with CIF2. Quantitative biochemical comparisons reveal that GSO1/SGN3-CIF2 represents one of the strongest receptor-ligand pairs known in plants. Multiple missense mutations are required to block CIF2 binding in vitro and GSO1/SGN3 function in vivo. Using structure-guided sequence analysis we uncover previously uncharacterized CIF peptides conserved among higher plants. Quantitative binding assays with known and novel CIFs suggest that the homologous LRR-RKs GSO1/SGN3 and GSO2 have evolved unique peptide binding properties to control different developmental processes. A quantitative biochemical interaction screen, a CIF peptide antagonist and genetic analyses together implicate SERK proteins as essential coreceptor kinases required for GSO1/SGN3 and GSO2 receptor activation. Our work provides a mechanistic framework for the recognition of sequence-divergent peptide hormones in plants. | ||
| + | |||
| + | Molecular mechanism for the recognition of sequence-divergent CIF peptides by the plant receptor kinases GSO1/SGN3 and GSO2.,Okuda S, Fujita S, Moretti A, Hohmann U, Doblas VG, Ma Y, Pfister A, Brandt B, Geldner N, Hothorn M Proc Natl Acad Sci U S A. 2020 Feb 4;117(5):2693-2703. doi:, 10.1073/pnas.1911553117. Epub 2020 Jan 21. PMID:31964818<ref>PMID:31964818</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6s6q" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Arath]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Non-specific serine/threonine protein kinase]] | [[Category: Non-specific serine/threonine protein kinase]] | ||
Revision as of 07:32, 19 February 2020
Crystal structure of the LRR ectodomain of the plant membrane receptor kinase GASSHO1/SCHENGEN3 from Arabidopsis thaliana in complex with CASPARIAN STRIP INTEGRITY FACTOR 2.
| |||||||||||
