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| | ==the plant peptide hormone receptor complex in arabidopsis== | | ==the plant peptide hormone receptor complex in arabidopsis== |
| - | <StructureSection load='4z64' size='340' side='right' caption='[[4z64]], [[Resolution|resolution]] 2.66Å' scene=''> | + | <StructureSection load='4z64' size='340' side='right'caption='[[4z64]], [[Resolution|resolution]] 2.66Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4z64]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z64 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Z64 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4z64]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis Arabidopsis] and [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z64 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z64 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>, <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]] 2.659Å</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=SO4:SULFATE+ION'>SO4</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">[[4z5w|4z5w]], [[4z61|4z61]], [[4z62|4z62]], [[4z63|4z63]]</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=4z64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z64 OCA], [https://pdbe.org/4z64 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z64 RCSB], [https://www.ebi.ac.uk/pdbsum/4z64 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z64 ProSAT]</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=4z64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z64 OCA], [http://pdbe.org/4z64 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4z64 RCSB], [http://www.ebi.ac.uk/pdbsum/4z64 PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PSKR1_ARATH PSKR1_ARATH]] Phytosulfokine receptor with a serine/threonine-protein kinase activity. Regulates, in response to phytosulfokine binding, a signaling cascade involved in plant cell differentiation, organogenesis, somatic embryogenesis, cellular proliferation and plant growth. Not involved in PSY perception.<ref>PMID:16829587</ref> <ref>PMID:17989228</ref> [[http://www.uniprot.org/uniprot/SERK1_ARATH SERK1_ARATH]] Dual specificity kinase acting on both serine/threonine- and tyrosine-containing substrates. Phosphorylates BRI1 on 'Ser-887' and CDC48 on at least one threonine residue and on 'Ser-41'. Confers embryogenic competence. Acts redundantly with SERK2 as a control point for sporophytic development controlling male gametophyte production. Involved in the brassinolide signaling pathway.<ref>PMID:11509554</ref> <ref>PMID:17693538</ref> | + | [https://www.uniprot.org/uniprot/PSKR1_ARATH PSKR1_ARATH] Phytosulfokine receptor with a serine/threonine-protein kinase activity. Regulates, in response to phytosulfokine binding, a signaling cascade involved in plant cell differentiation, organogenesis, somatic embryogenesis, cellular proliferation and plant growth. Not involved in PSY perception.<ref>PMID:16829587</ref> <ref>PMID:17989228</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: Non-specific serine/threonine protein kinase]] | + | [[Category: Arabidopsis]] |
| - | [[Category: Chai, J]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Han, Z]] | + | [[Category: Large Structures]] |
| - | [[Category: Wang, J]] | + | [[Category: Chai J]] |
| - | [[Category: Hormone]] | + | [[Category: Han Z]] |
| - | [[Category: Hormone receptor complex]] | + | [[Category: Wang J]] |
| Structural highlights
Function
PSKR1_ARATH Phytosulfokine receptor with a serine/threonine-protein kinase activity. Regulates, in response to phytosulfokine binding, a signaling cascade involved in plant cell differentiation, organogenesis, somatic embryogenesis, cellular proliferation and plant growth. Not involved in PSY perception.[1] [2]
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Matsubayashi Y, Ogawa M, Kihara H, Niwa M, Sakagami Y. Disruption and overexpression of Arabidopsis phytosulfokine receptor gene affects cellular longevity and potential for growth. Plant Physiol. 2006 Sep;142(1):45-53. Epub 2006 Jul 7. PMID:16829587 doi:http://dx.doi.org/10.1104/pp.106.081109
- ↑ Amano Y, Tsubouchi H, Shinohara H, Ogawa M, Matsubayashi Y. Tyrosine-sulfated glycopeptide involved in cellular proliferation and expansion in Arabidopsis. Proc Natl Acad Sci U S A. 2007 Nov 13;104(46):18333-8. Epub 2007 Nov 7. PMID:17989228 doi:http://dx.doi.org/10.1073/pnas.0706403104
- ↑ 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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