3jrq

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{{STRUCTURE_3jrq| PDB=3jrq | SCENE= }}
 
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===Crystal structure of (+)-ABA-bound PYL1 in complex with ABI1===
 
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{{ABSTRACT_PUBMED_19855379}}
 
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==Function==
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==Crystal structure of (+)-ABA-bound PYL1 in complex with ABI1==
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[[http://www.uniprot.org/uniprot/P2C56_ARATH P2C56_ARATH]] Key component and repressor of the abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomatal closure, osmotic water permeability of the plasma membrane (Pos), drought-induced resistance and rhizogenesis, response to glucose, high light stress, seed germination and inhibition of vegetative growth. During the stomatal closure regulation, modulates the inward calcium-channel permeability as well as the actin reorganization in guard cells in response to ABA. Involved in the resistance to the bacterial pathogen Pseudomonas syringae pv. tomato. Controls negatively fibrillin expression that is involved in mediating ABA-induced photoprotection. May be involved in ABA content regulation. Plays a role in the Pro accumulation in response to reduced water availability (low water potential). Required for the ABA negative regulation of the ethylene-induced hyponastic growth. Involved in acquired thermotolerance of root growth and seedling survival. Activates/represses SRK2E/OST1 in response to ABA-dependent stimuli, especially in stomata closure regulation involving SLAC1.<ref>PMID:12228349</ref><ref>PMID:1834244</ref><ref>PMID:16652949</ref><ref>PMID:8492808</ref><ref>PMID:12232276</ref><ref>PMID:12232124</ref><ref>PMID:7568166</ref><ref>PMID:12228349</ref><ref>PMID:8898906</ref><ref>PMID:8771791</ref><ref>PMID:9108297</ref><ref>PMID:9090884</ref><ref>PMID:9165752</ref><ref>PMID:9161030</ref><ref>PMID:9263461</ref><ref>PMID:9351242</ref><ref>PMID:9276963</ref><ref>PMID:9448270</ref><ref>PMID:10645425</ref><ref>PMID:10488243</ref><ref>PMID:10521520</ref><ref>PMID:10950871</ref><ref>PMID:10872217</ref><ref>PMID:11707572</ref><ref>PMID:11208021</ref><ref>PMID:11587514</ref><ref>PMID:11289613</ref><ref>PMID:11701885</ref><ref>PMID:12194854</ref><ref>PMID:12065416</ref><ref>PMID:12432076</ref><ref>PMID:12047634</ref><ref>PMID:12713537</ref><ref>PMID:14576281</ref><ref>PMID:14596925</ref><ref>PMID:12609042</ref><ref>PMID:15144382</ref><ref>PMID:15197253</ref><ref>PMID:15618419</ref><ref>PMID:15923322</ref><ref>PMID:16365038</ref><ref>PMID:16339784</ref><ref>PMID:16571665</ref><ref>PMID:16798945</ref><ref>PMID:16614222</ref><ref>PMID:17304219</ref><ref>PMID:17158582</ref><ref>PMID:18298671</ref><ref>PMID:19955405</ref>
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<StructureSection load='3jrq' size='340' side='right'caption='[[3jrq]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3jrq]] 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=3JRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JRQ FirstGlance]. <br>
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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]] 2.1&#8491;</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></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=3jrq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jrq OCA], [https://pdbe.org/3jrq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jrq RCSB], [https://www.ebi.ac.uk/pdbsum/3jrq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jrq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/P2C56_ARATH P2C56_ARATH] Key component and repressor of the abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomatal closure, osmotic water permeability of the plasma membrane (Pos), drought-induced resistance and rhizogenesis, response to glucose, high light stress, seed germination and inhibition of vegetative growth. During the stomatal closure regulation, modulates the inward calcium-channel permeability as well as the actin reorganization in guard cells in response to ABA. Involved in the resistance to the bacterial pathogen Pseudomonas syringae pv. tomato. Controls negatively fibrillin expression that is involved in mediating ABA-induced photoprotection. May be involved in ABA content regulation. Plays a role in the Pro accumulation in response to reduced water availability (low water potential). Required for the ABA negative regulation of the ethylene-induced hyponastic growth. Involved in acquired thermotolerance of root growth and seedling survival. Activates/represses SRK2E/OST1 in response to ABA-dependent stimuli, especially in stomata closure regulation involving SLAC1.<ref>PMID:12228349</ref> <ref>PMID:1834244</ref> <ref>PMID:16652949</ref> <ref>PMID:8492808</ref> <ref>PMID:12232276</ref> <ref>PMID:12232124</ref> <ref>PMID:7568166</ref> <ref>PMID:12228349</ref> <ref>PMID:8898906</ref> <ref>PMID:8771791</ref> <ref>PMID:9108297</ref> <ref>PMID:9090884</ref> <ref>PMID:9165752</ref> <ref>PMID:9161030</ref> <ref>PMID:9263461</ref> <ref>PMID:9351242</ref> <ref>PMID:9276963</ref> <ref>PMID:9448270</ref> <ref>PMID:10645425</ref> <ref>PMID:10488243</ref> <ref>PMID:10521520</ref> <ref>PMID:10950871</ref> <ref>PMID:10872217</ref> <ref>PMID:11707572</ref> <ref>PMID:11208021</ref> <ref>PMID:11587514</ref> <ref>PMID:11289613</ref> <ref>PMID:11701885</ref> <ref>PMID:12194854</ref> <ref>PMID:12065416</ref> <ref>PMID:12432076</ref> <ref>PMID:12047634</ref> <ref>PMID:12713537</ref> <ref>PMID:14576281</ref> <ref>PMID:14596925</ref> <ref>PMID:12609042</ref> <ref>PMID:15144382</ref> <ref>PMID:15197253</ref> <ref>PMID:15618419</ref> <ref>PMID:15923322</ref> <ref>PMID:16365038</ref> <ref>PMID:16339784</ref> <ref>PMID:16571665</ref> <ref>PMID:16798945</ref> <ref>PMID:16614222</ref> <ref>PMID:17304219</ref> <ref>PMID:17158582</ref> <ref>PMID:18298671</ref> <ref>PMID:19955405</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jr/3jrq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3jrq ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The phytohormone abscisic acid (ABA) mediates the adaptation of plants to environmental stresses such as drought and regulates developmental signals such as seed maturation. Within plants, the PYR/PYL/RCAR family of START proteins receives ABA to inhibit the phosphatase activity of the group-A protein phosphatases 2C (PP2Cs), which are major negative regulators in ABA signalling. Here we present the crystal structures of the ABA receptor PYL1 bound with (+)-ABA, and the complex formed by the further binding of (+)-ABA-bound PYL1 with the PP2C protein ABI1. PYL1 binds (+)-ABA using the START-protein-specific ligand-binding site, thereby forming a hydrophobic pocket on the surface of the closed lid. (+)-ABA-bound PYL1 tightly interacts with a PP2C domain of ABI1 by using the hydrophobic pocket to cover the active site of ABI1 like a plug. Our results reveal the structural basis of the mechanism of (+)-ABA-dependent inhibition of ABI1 by PYL1 in ABA signalling.
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==About this Structure==
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Structural basis of abscisic acid signalling.,Miyazono K, Miyakawa T, Sawano Y, Kubota K, Kang HJ, Asano A, Miyauchi Y, Takahashi M, Zhi Y, Fujita Y, Yoshida T, Kodaira KS, Yamaguchi-Shinozaki K, Tanokura M Nature. 2009 Dec 3;462(7273):609-14. PMID:19855379<ref>PMID:19855379</ref>
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[[3jrq]] 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=3JRQ OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:019855379</ref><references group="xtra"/><references/>
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</div>
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<div class="pdbe-citations 3jrq" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Abscisic acid receptor 3D structures|Abscisic acid receptor 3D structures]]
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*[[Protein phosphatase 3D structures|Protein phosphatase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
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[[Category: Phosphoprotein phosphatase]]
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[[Category: Large Structures]]
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[[Category: Kubota, K.]]
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[[Category: Kubota K]]
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[[Category: Miyakawa, T.]]
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[[Category: Miyakawa T]]
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[[Category: Miyazono, K.]]
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[[Category: Miyazono K]]
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[[Category: Sawano, Y.]]
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[[Category: Sawano Y]]
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[[Category: Tanokura, M.]]
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[[Category: Tanokura M]]
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[[Category: Abi1]]
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[[Category: Abscisic acid]]
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[[Category: Abscisic acid signaling pathway]]
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[[Category: Cell membrane]]
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[[Category: Hydrolase]]
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[[Category: Hydrolase-hormone receptor complex]]
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[[Category: Magnesium]]
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[[Category: Manganese]]
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[[Category: Membrane]]
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[[Category: Metal-binding]]
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[[Category: Nucleus]]
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[[Category: Plant hormone receptor]]
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[[Category: Protein phosphatase]]
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[[Category: Pyl1]]
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[[Category: Type 2c protein phosphatase]]
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Current revision

Crystal structure of (+)-ABA-bound PYL1 in complex with ABI1

PDB ID 3jrq

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