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==Crystal structure of the PYR1 Abscisic Acid receptor in complex with the HAB1 type 2C phosphatase catalytic domain==
==Crystal structure of the PYR1 Abscisic Acid receptor in complex with the HAB1 type 2C phosphatase catalytic domain==
<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 ==
<table><tr><td colspan='2'>[[3qn1]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QN1 FirstGlance]. <br>
<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>
</td></tr><tr id='ligand'><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=MN:MANGANESE+(II)+ION'>MN</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]] 1.8&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3k90|3k90]], [[3k3k|3k3k]], [[3nmt|3nmt]], [[3njo|3njo]]</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>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABIP6, At4g17870, PYR1, RCAR11, T6K21.50 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana]), At1g72770, F28P22.4, HAB1, P2C-HA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])</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>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </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=3qn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qn1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qn1 RCSB], [http://www.ebi.ac.uk/pdbsum/3qn1 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>  [[http://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> 
[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>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
 
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>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[ABA-regulated Protein Phosphatase 2C|ABA-regulated Protein Phosphatase 2C]]
*[[Abscisic acid receptor 3D structures|Abscisic acid receptor 3D structures]]
*[[PYR/PYL/RCAR family of ABA receptors|PYR/PYL/RCAR family of ABA receptors]]
*[[Protein phosphatase 3D structures|Protein phosphatase 3D structures]]
*[[Protein phosphatase|Protein phosphatase]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Phosphoprotein phosphatase]]
[[Category: Large Structures]]
[[Category: Betz, K]]
[[Category: Betz K]]
[[Category: Dupeux, F]]
[[Category: Dupeux F]]
[[Category: Marquez, J A]]
[[Category: Marquez JA]]
[[Category: Santiago, J]]
[[Category: Santiago J]]
[[Category: Abiotic stress]]
[[Category: Abscisic acid binding]]
[[Category: Abscisic acid hormone receptor]]
[[Category: Bet v domain]]
[[Category: Intracellular]]
[[Category: Nucleus]]
[[Category: Plant stress response]]
[[Category: Pp2c]]
[[Category: Protein binding]]
[[Category: Pyr/pyl/rcar]]
[[Category: Start domain]]
[[Category: Type 2c protein phosphatase]]
[[Category: Type 2c protein phosphatase binding]]

Latest revision as of 14:51, 14 March 2024

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

Structural highlights

3qn1 is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2] [3]

See Also

References

  1. ↑ Santiago J, Rodrigues A, Saez A, Rubio S, Antoni R, Dupeux F, Park SY, Marquez JA, Cutler SR, Rodriguez PL. Modulation of drought resistance by the abscisic acid receptor PYL5 through inhibition of clade A PP2Cs. Plant J. 2009 Nov;60(4):575-88. doi: 10.1111/j.1365-313X.2009.03981.x. Epub 2009 , Jul 16. PMID:19624469 doi:10.1111/j.1365-313X.2009.03981.x
  2. ↑ Park SY, Fung P, Nishimura N, Jensen DR, Fujii H, Zhao Y, Lumba S, Santiago J, Rodrigues A, Chow TF, Alfred SE, Bonetta D, Finkelstein R, Provart NJ, Desveaux D, Rodriguez PL, McCourt P, Zhu JK, Schroeder JI, Volkman BF, Cutler SR. Abscisic acid inhibits type 2C protein phosphatases via the PYR/PYL family of START proteins. Science. 2009 May 22;324(5930):1068-71. doi: 10.1126/science.1173041. Epub 2009, Apr 30. PMID:19407142 doi:10.1126/science.1173041
  3. ↑ Szostkiewicz I, Richter K, Kepka M, Demmel S, Ma Y, Korte A, Assaad FF, Christmann A, Grill E. Closely related receptor complexes differ in their ABA selectivity and sensitivity. Plant J. 2010 Jan;61(1):25-35. doi: 10.1111/j.1365-313X.2009.04025.x. Epub 2009, Sep 21. PMID:19769575 doi:10.1111/j.1365-313X.2009.04025.x

3qn1, resolution 1.80Å

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