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| | <StructureSection load='4z5w' size='340' side='right'caption='[[4z5w]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='4z5w' size='340' side='right'caption='[[4z5w]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4z5w]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Dauca Dauca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z5W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Z5W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4z5w]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis Arabidopsis] and [https://en.wikipedia.org/wiki/Daucus_carota Daucus carota]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z5W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z5W FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.2Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=TYS:O-SULFO-L-TYROSINE'>TYS</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4z61|4z61]], [[4z62|4z62]], [[4z63|4z63]], [[4z64|4z64]]</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=4z5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z5w OCA], [https://pdbe.org/4z5w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z5w RCSB], [https://www.ebi.ac.uk/pdbsum/4z5w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z5w ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PSKR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4039 DAUCA])</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=4z5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z5w OCA], [http://pdbe.org/4z5w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4z5w RCSB], [http://www.ebi.ac.uk/pdbsum/4z5w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4z5w ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PSKR1_DAUCA PSKR1_DAUCA]] Phytosulfokine receptor with a serine/threonine-protein kinase activity. Regulates, in response to phytosulfokine binding, a signaling cascade involved in plant cell differentiation, organogenesis and somatic embryogenesis.<ref>PMID:12029134</ref> | + | [https://www.uniprot.org/uniprot/PSKR1_DAUCA PSKR1_DAUCA] Phytosulfokine receptor with a serine/threonine-protein kinase activity. Regulates, in response to phytosulfokine binding, a signaling cascade involved in plant cell differentiation, organogenesis and somatic embryogenesis.<ref>PMID:12029134</ref> |
| | <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: Dauca]] | + | [[Category: Arabidopsis]] |
| | + | [[Category: Daucus carota]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Non-specific serine/threonine protein kinase]]
| + | [[Category: Chai J]] |
| - | [[Category: Chai, J]] | + | [[Category: Han Z]] |
| - | [[Category: Han, Z]] | + | [[Category: Wang J]] |
| - | [[Category: Wang, J]] | + | |
| - | [[Category: Hormone]]
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| - | [[Category: Receptor]]
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| Structural highlights
Function
PSKR1_DAUCA Phytosulfokine receptor with a serine/threonine-protein kinase activity. Regulates, in response to phytosulfokine binding, a signaling cascade involved in plant cell differentiation, organogenesis and somatic embryogenesis.[1]
Publication Abstract from PubMed
Phytosulfokine (PSK) is a disulfated pentapeptide that has a ubiquitous role in plant growth and development. PSK is perceived by its receptor PSKR, a leucine-rich repeat receptor kinase (LRR-RK). The mechanisms underlying the recognition of PSK, the activation of PSKR and the identity of the components downstream of the initial binding remain elusive. Here we report the crystal structures of the extracellular LRR domain of PSKR in free, PSK- and co-receptor-bound forms. The structures reveal that PSK interacts mainly with a beta-strand from the island domain of PSKR, forming an anti-beta-sheet. The two sulfate moieties of PSK interact directly with PSKR, sensitizing PSKR recognition of PSK. Supported by biochemical, structural and genetic evidence, PSK binding enhances PSKR heterodimerization with the somatic embryogenesis receptor-like kinases (SERKs). However, PSK is not directly involved in PSKR-SERK interaction but stabilizes PSKR island domain for recruitment of a SERK. Our data reveal the structural basis for PSKR recognition of PSK and allosteric activation of PSKR by PSK, opening up new avenues for the design of PSKR-specific small molecules.
Allosteric receptor activation by the plant peptide hormone phytosulfokine.,Wang J, Li H, Han Z, Zhang H, Wang T, Lin G, Chang J, Yang W, Chai J Nature. 2015 Sep 10;525(7568):265-8. doi: 10.1038/nature14858. Epub 2015 Aug 26. PMID:26308901[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Matsubayashi Y, Ogawa M, Morita A, Sakagami Y. An LRR receptor kinase involved in perception of a peptide plant hormone, phytosulfokine. Science. 2002 May 24;296(5572):1470-2. PMID:12029134 doi:http://dx.doi.org/10.1126/science.1069607
- ↑ Wang J, Li H, Han Z, Zhang H, Wang T, Lin G, Chang J, Yang W, Chai J. Allosteric receptor activation by the plant peptide hormone phytosulfokine. Nature. 2015 Sep 10;525(7568):265-8. doi: 10.1038/nature14858. Epub 2015 Aug 26. PMID:26308901 doi:http://dx.doi.org/10.1038/nature14858
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