3qn1

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Current revision (11:51, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3qn1' size='340' side='right'caption='[[3qn1]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3qn1' size='340' side='right'caption='[[3qn1]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qn1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QN1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QN1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qn1]] 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=3QN1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QN1 FirstGlance]. <br>
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</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=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3k90|3k90]], [[3k3k|3k3k]], [[3nmt|3nmt]], [[3njo|3njo]]</div></td></tr>
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<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=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABIP6, At4g17870, PYR1, RCAR11, T6K21.50 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH]), At1g72770, F28P22.4, HAB1, P2C-HA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qn1 OCA], [https://pdbe.org/3qn1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qn1 RCSB], [https://www.ebi.ac.uk/pdbsum/3qn1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qn1 ProSAT]</span></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=3qn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qn1 OCA], [https://pdbe.org/3qn1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qn1 RCSB], [https://www.ebi.ac.uk/pdbsum/3qn1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qn1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/PYR1_ARATH PYR1_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:19624469</ref> <ref>PMID:19407142</ref> <ref>PMID:19769575</ref> [[https://www.uniprot.org/uniprot/P2C16_ARATH P2C16_ARATH]] Key component and repressor of the abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomatal closure, seed germination and inhibition of vegetative growth. Confers enhanced sensitivity to drought.<ref>PMID:14731256</ref> <ref>PMID:16876791</ref> <ref>PMID:16798945</ref> <ref>PMID:19033529</ref>
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[https://www.uniprot.org/uniprot/PYR1_ARATH PYR1_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:19624469</ref> <ref>PMID:19407142</ref> <ref>PMID:19769575</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The plant hormone abscisic acid (ABA) plays a crucial role in the control of the stress response and the regulation of plant growth and development. ABA binding to PYR/PYL/RCAR intracellular receptors leads to inhibition of key negative regulators of ABA signaling, i.e. clade A protein phosphatases type 2C (PP2Cs) such as ABI1 and HAB1, causing the activation of the ABA signaling pathway. In order to gain further understanding on the mechanism of hormone perception, PP2C inhibition and its implications for ABA signaling, we have performed a structural and functional analysis of the PYR1-ABA-HAB1 complex. Based on structural data, we generated a gain-of-function mutation in a critical residue of the phosphatase, hab1W385A, which abolished ABA-dependent receptor-mediated PP2C inhibition without impairing basal PP2C activity. As a result, hab1W385A caused constitutive inactivation of the protein kinase OST1 even in the presence of ABA and PYR/PYL proteins, in contrast to the receptor-sensitive HAB1, and therefore hab1W385A qualifies as a hypermorphic mutation. Expression of hab1W385A in Arabidopsis thaliana plants leads to a strong, dominant ABA-insensitivity, which demonstrates that this conserved Trp residue can be targeted for the generation of dominant clade A PP2C alleles. Moreover, our data highlight the critical role of molecular interactions mediated by Trp385 equivalent residues for clade A PP2C function in vivo and the mechanism of ABA perception and signaling.
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Modulation of ABA signaling in vivo by an engineered receptor-insensitive PP2C allele.,Dupeux F, Antoni R, Betz K, Santiago J, Gonzalez-Guzman M, Rodriguez L, Rubio S, Park SY, Cutler S, Rodriguez PL, Marquez J Plant Physiol. 2011 Mar 14. PMID:21357183<ref>PMID:21357183</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3qn1" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arath]]
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[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Phosphoprotein phosphatase]]
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[[Category: Betz K]]
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[[Category: Betz, K]]
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[[Category: Dupeux F]]
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[[Category: Dupeux, F]]
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[[Category: Marquez JA]]
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[[Category: Marquez, J A]]
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[[Category: Santiago J]]
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[[Category: Santiago, J]]
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[[Category: Abiotic stress]]
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[[Category: Abscisic acid binding]]
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[[Category: Abscisic acid hormone receptor]]
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[[Category: Bet v domain]]
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[[Category: Intracellular]]
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[[Category: Nucleus]]
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[[Category: Plant stress response]]
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[[Category: Pp2c]]
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[[Category: Protein binding]]
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[[Category: Pyr/pyl/rcar]]
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[[Category: Start domain]]
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[[Category: Type 2c protein phosphatase]]
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[[Category: Type 2c protein phosphatase binding]]
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Current revision

Crystal structure of the PYR1 Abscisic Acid receptor in complex with the HAB1 type 2C phosphatase catalytic domain

PDB ID 3qn1

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