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==X-ray crystal structure of the PYL2(V114I)-pyrabactin A complex== | ==X-ray crystal structure of the PYL2(V114I)-pyrabactin A complex== | ||
<StructureSection load='3nj1' size='340' side='right' caption='[[3nj1]], [[Resolution|resolution]] 1.95Å' scene=''> | <StructureSection load='3nj1' size='340' side='right'caption='[[3nj1]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3nj1]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3nj1]] is a 1 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=3NJ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NJ1 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=P2M:N-(PYRIDIN-2-YLMETHYL)NAPHTHALENE-1-SULFONAMIDE'>P2M</scene>, <scene name='pdbligand=PYV:4-BROMO-N-(PYRIDIN-2-YLMETHYL)NAPHTHALENE-1-SULFONAMIDE'>PYV</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]] 1.948Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=P2M:N-(PYRIDIN-2-YLMETHYL)NAPHTHALENE-1-SULFONAMIDE'>P2M</scene>, <scene name='pdbligand=PYV:4-BROMO-N-(PYRIDIN-2-YLMETHYL)NAPHTHALENE-1-SULFONAMIDE'>PYV</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=3nj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nj1 OCA], [https://pdbe.org/3nj1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nj1 RCSB], [https://www.ebi.ac.uk/pdbsum/3nj1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nj1 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nj/3nj1_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nj/3nj1_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
| Line 32: | Line 31: | ||
==See Also== | ==See Also== | ||
*[[ | *[[Abscisic acid receptor 3D structures|Abscisic acid receptor 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Arabidopsis thaliana]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Bingman CA]] | ||
[[Category: | [[Category: Burgie ES]] | ||
[[Category: Cutler | [[Category: Cutler SR]] | ||
[[Category: Jensen | [[Category: Jensen DR]] | ||
[[Category: Peterson | [[Category: Peterson FC]] | ||
[[Category: Phillips | [[Category: Phillips Jr GN]] | ||
[[Category: Volkman | [[Category: Volkman BF]] | ||
Latest revision as of 12:16, 6 September 2023
X-ray crystal structure of the PYL2(V114I)-pyrabactin A complexX-ray crystal structure of the PYL2(V114I)-pyrabactin A complex
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] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedChanging environmental conditions and lessening fresh water supplies have sparked intense interest in understanding and manipulating abscisic acid (ABA) signaling, which controls adaptive responses to drought and other abiotic stressors. We recently discovered a selective ABA agonist, pyrabactin, and used it to discover its primary target PYR1, the founding member of the PYR/PYL family of soluble ABA receptors. To understand pyrabactin's selectivity, we have taken a combined structural, chemical and genetic approach. We show that subtle differences between receptor binding pockets control ligand orientation between productive and nonproductive modes. Nonproductive binding occurs without gate closure and prevents receptor activation. Observations in solution show that these orientations are in rapid equilibrium that can be shifted by mutations to control maximal agonist activity. Our results provide a robust framework for the design of new agonists and reveal a new mechanism for agonist selectivity. Structural basis for selective activation of ABA receptors.,Peterson FC, Burgie ES, Park SY, Jensen DR, Weiner JJ, Bingman CA, Chang CE, Cutler SR, Phillips GN Jr, Volkman BF Nat Struct Mol Biol. 2010 Sep;17(9):1109-13. Epub 2010 Aug 22. PMID:20729860[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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