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{{STRUCTURE_3k90|  PDB=3k90  |  SCENE=  }}
===The Abscisic acid receptor PYR1 in complex with Abscisic Acid===
{{ABSTRACT_PUBMED_19898494}}


==About this Structure==
==The Abscisic acid receptor PYR1 in complex with Abscisic Acid==
[[3k90]] is a 4 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=3K90 OCA].  
<StructureSection load='3k90' size='340' side='right'caption='[[3k90]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3k90]] is a 4 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=3K90 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K90 FirstGlance]. <br>
</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&#8491;</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=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=3k90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k90 OCA], [https://pdbe.org/3k90 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k90 RCSB], [https://www.ebi.ac.uk/pdbsum/3k90 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k90 ProSAT]</span></td></tr>
</table>
== Function ==
[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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k9/3k90_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3k90 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The plant hormone abscisic acid (ABA) has a central role in coordinating the adaptive response in situations of decreased water availability as well as the regulation of plant growth and development. Recently, a 14-member family of intracellular ABA receptors, named PYR/PYL/RCAR, has been identified. These proteins inhibit in an ABA-dependent manner the activity of a family of key negative regulators of the ABA signalling pathway: the group-A protein phosphatases type 2C (PP2Cs). Here we present the crystal structure of Arabidopsis thaliana PYR1, which consists of a dimer in which one of the subunits is bound to ABA. In the ligand-bound subunit, the loops surrounding the entry to the binding cavity fold over the ABA molecule, enclosing it inside, whereas in the empty subunit they form a channel leaving an open access to the cavity, indicating that conformational changes in these loops have a critical role in the stabilization of the hormone-receptor complex. By providing structural details on the ABA-binding pocket, this work paves the way for the development of new small molecules able to activate the plant stress response.


==Reference==
The abscisic acid receptor PYR1 in complex with abscisic acid.,Santiago J, Dupeux F, Round A, Antoni R, Park SY, Jamin M, Cutler SR, Rodriguez PL, Marquez JA Nature. 2009 Dec 3;462(7273):665-8. Epub 2009 Nov 8. PMID:19898494<ref>PMID:19898494</ref>
<ref group="xtra">PMID:019898494</ref><references group="xtra"/><references/>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3k90" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Abscisic acid receptor 3D structures|Abscisic acid receptor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Dupeux, F D.]]
[[Category: Large Structures]]
[[Category: Marquez, J A.]]
[[Category: Dupeux FD]]
[[Category: Rodriguez, P L.]]
[[Category: Marquez JA]]
[[Category: Santiago, J.]]
[[Category: Rodriguez PL]]
[[Category: Bet v i domain]]
[[Category: Santiago J]]
[[Category: Gene regulator]]
[[Category: Hormone]]
[[Category: Hormone receptor]]
[[Category: Hormone-receptor complex]]
[[Category: Hydrolase regulator]]
[[Category: Plant protein]]
[[Category: Regulator of protein phosphatase type 2c]]
[[Category: Signaling protein]]
[[Category: Start domain]]
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