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==Crystal structure of abscisic acid bound PYL2 in complex with type 2C protein phosphatase ABI2== | ==Crystal structure of abscisic acid bound PYL2 in complex with type 2C protein phosphatase ABI2== | ||
<StructureSection load='3ujl' size='340' side='right' caption='[[3ujl]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='3ujl' size='340' side='right'caption='[[3ujl]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ujl]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3ujl]] 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=3UJL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UJL FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A8S:(2Z,4E)-5-[(1S)-1-HYDROXY-2,6,6-TRIMETHYL-4-OXOCYCLOHEX-2-EN-1-YL]-3-METHYLPENTA-2,4-DIENOIC+ACID'>A8S</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A8S:(2Z,4E)-5-[(1S)-1-HYDROXY-2,6,6-TRIMETHYL-4-OXOCYCLOHEX-2-EN-1-YL]-3-METHYLPENTA-2,4-DIENOIC+ACID'>A8S</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ujl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ujl OCA], [https://pdbe.org/3ujl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ujl RCSB], [https://www.ebi.ac.uk/pdbsum/3ujl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ujl ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
<table> | [https://www.uniprot.org/uniprot/PYL2_ARATH PYL2_ARATH] Receptor for abscisic acid (ABA) required for ABA-mediated responses such as stomatal closure and germination inhibition. Inhibits the activity of group-A protein phosphatases type 2C (PP2Cs) when activated by ABA.<ref>PMID:19898420</ref> <ref>PMID:19893533</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 15: | Line 16: | ||
Molecular mimicry regulates ABA signaling by SnRK2 kinases and PP2C phosphatases.,Soon FF, Ng LM, Zhou XE, West GM, Kovach A, Tan MH, Suino-Powell KM, He Y, Xu Y, Chalmers MJ, Brunzelle JS, Zhang H, Yang H, Jiang H, Li J, Yong EL, Cutler S, Zhu JK, Griffin PR, Melcher K, Xu HE Science. 2012 Jan 6;335(6064):85-8. Epub 2011 Nov 24. PMID:22116026<ref>PMID:22116026</ref> | Molecular mimicry regulates ABA signaling by SnRK2 kinases and PP2C phosphatases.,Soon FF, Ng LM, Zhou XE, West GM, Kovach A, Tan MH, Suino-Powell KM, He Y, Xu Y, Chalmers MJ, Brunzelle JS, Zhang H, Yang H, Jiang H, Li J, Yong EL, Cutler S, Zhu JK, Griffin PR, Melcher K, Xu HE Science. 2012 Jan 6;335(6064):85-8. Epub 2011 Nov 24. PMID:22116026<ref>PMID:22116026</ref> | ||
From | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3ujl" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[ | *[[Abscisic acid receptor 3D structures|Abscisic acid receptor 3D structures]] | ||
*[[Protein phosphatase 3D structures|Protein phosphatase 3D structures]] | |||
*[[Protein phosphatase|Protein phosphatase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 28: | Line 28: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Brunzelle | [[Category: Brunzelle JS]] | ||
[[Category: He | [[Category: He Y]] | ||
[[Category: Kovach | [[Category: Kovach A]] | ||
[[Category: Li | [[Category: Li J]] | ||
[[Category: Melcher | [[Category: Melcher K]] | ||
[[Category: Ng | [[Category: Ng L-M]] | ||
[[Category: Soon | [[Category: Soon F-F]] | ||
[[Category: Suino-Powell | [[Category: Suino-Powell KM]] | ||
[[Category: Tan | [[Category: Tan MHE]] | ||
[[Category: Xu | [[Category: Xu HE]] | ||
[[Category: Xu | [[Category: Xu Y]] | ||
[[Category: Zhou | [[Category: Zhou XE]] | ||
Latest revision as of 11:11, 9 October 2024
Crystal structure of abscisic acid bound PYL2 in complex with type 2C protein phosphatase ABI2Crystal structure of abscisic acid bound PYL2 in complex with type 2C protein phosphatase ABI2
Structural highlights
FunctionPYL2_ARATH Receptor for abscisic acid (ABA) required for ABA-mediated responses such as stomatal closure and germination inhibition. Inhibits the activity of group-A protein phosphatases type 2C (PP2Cs) when activated by ABA.[1] [2] Publication Abstract from PubMedAbscisic acid (ABA) is an essential hormone for plants to survive environmental stresses. At the center of the ABA signaling network is a subfamily of type 2C protein phosphatases (PP2Cs), which form exclusive interactions with ABA receptors and subfamily 2 Snfl-related kinase (SnRK2s). Here, we report a SnRK2-PP2C complex structure, which reveals marked similarity in PP2C recognition by SnRK2 and ABA receptors. In the complex, the kinase activation loop docks into the active site of PP2C, while the conserved ABA-sensing tryptophan of PP2C inserts into the kinase catalytic cleft, thus mimicking receptor-PP2C interactions. These structural results provide a simple mechanism that directly couples ABA binding to SnRK2 kinase activation and highlight a new paradigm of kinase-phosphatase regulation through mutual packing of their catalytic sites. Molecular mimicry regulates ABA signaling by SnRK2 kinases and PP2C phosphatases.,Soon FF, Ng LM, Zhou XE, West GM, Kovach A, Tan MH, Suino-Powell KM, He Y, Xu Y, Chalmers MJ, Brunzelle JS, Zhang H, Yang H, Jiang H, Li J, Yong EL, Cutler S, Zhu JK, Griffin PR, Melcher K, Xu HE Science. 2012 Jan 6;335(6064):85-8. Epub 2011 Nov 24. PMID:22116026[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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