4z64: Difference between revisions

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'''Unreleased structure'''


The entry 4z64 is ON HOLD until Paper Publication
==the plant peptide hormone receptor complex in arabidopsis==
<StructureSection load='4z64' size='340' side='right' caption='[[4z64]], [[Resolution|resolution]] 2.66&Aring;' scene=''>
== 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>
</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>
<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='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='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>
== 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>  
<div style="background-color:#fffaf0;">
== 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.


Authors: Chai, J.J., Wang, J.Z., Han, Z.F.
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<ref>PMID:26308901</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Wang, J.Z]]
<div class="pdbe-citations 4z64" style="background-color:#fffaf0;"></div>
[[Category: Chai, J.J]]
== References ==
[[Category: Han, Z.F]]
<references/>
__TOC__
</StructureSection>
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Chai, J]]
[[Category: Han, Z]]
[[Category: Wang, J]]
[[Category: Hormone]]
[[Category: Hormone receptor complex]]

Revision as of 18:08, 2 March 2016

the plant peptide hormone receptor complex in arabidopsisthe plant peptide hormone receptor complex in arabidopsis

Structural highlights

4z64 is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
NonStd Res:
Activity:Non-specific serine/threonine protein kinase, with EC number 2.7.11.1
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

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] [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.[3] [4]

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[5]

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

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ Shah K, Vervoort J, de Vries SC. Role of threonines in the Arabidopsis thaliana somatic embryogenesis receptor kinase 1 activation loop in phosphorylation. J Biol Chem. 2001 Nov 2;276(44):41263-9. Epub 2001 Aug 16. PMID:11509554 doi:10.1074/jbc.M102381200
  4. ↑ Aker J, Hesselink R, Engel R, Karlova R, Borst JW, Visser AJ, de Vries SC. In vivo hexamerization and characterization of the Arabidopsis AAA ATPase CDC48A complex using forster resonance energy transfer-fluorescence lifetime imaging microscopy and fluorescence correlation spectroscopy. Plant Physiol. 2007 Oct;145(2):339-50. Epub 2007 Aug 10. PMID:17693538 doi:10.1104/pp.107.103986
  5. ↑ 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

4z64, resolution 2.66Å

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