3rt2: Difference between revisions
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<StructureSection load='3rt2' size='340' side='right'caption='[[3rt2]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='3rt2' size='340' side='right'caption='[[3rt2]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3rt2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3rt2]] 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=3RT2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RT2 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</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=3rt2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rt2 OCA], [https://pdbe.org/3rt2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rt2 RCSB], [https://www.ebi.ac.uk/pdbsum/3rt2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rt2 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=3rt2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rt2 OCA], [https://pdbe.org/3rt2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rt2 RCSB], [https://www.ebi.ac.uk/pdbsum/3rt2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rt2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/PYL10_ARATH PYL10_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 (By similarity). | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Arabidopsis thaliana]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Hao | [[Category: Hao Q]] | ||
[[Category: Li | [[Category: Li W]] | ||
[[Category: Wang | [[Category: Wang J]] | ||
[[Category: Wang | [[Category: Wang L]] | ||
[[Category: Yan | [[Category: Yan C]] | ||
[[Category: Yan | [[Category: Yan N]] | ||
[[Category: Yin | [[Category: Yin P]] | ||
Latest revision as of 20:19, 1 November 2023
Crystal structure of apo-PYL10Crystal structure of apo-PYL10
Structural highlights
FunctionPYL10_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 (By similarity). Publication Abstract from PubMedPYR1/PYL/RCAR proteins (PYLs) are confirmed abscisic acid (ABA) receptors, which inhibit protein phosphatase 2C (PP2C) upon binding to ABA. Arabidopsis thaliana has 14 PYLs, yet their functional distinction remains unclear. Here, we report systematic biochemical characterization of PYLs. A subclass of PYLs, represented by PYL10, inhibited PP2C in the absence of any ligand. Crystal structures of PYL10, both in the free form and in the HAB1 (PP2C)-bound state, revealed the structural basis for its constitutive activity. Structural-guided biochemical analyses revealed that ABA-independent inhibition of PP2C requires the PYLs to exist in a monomeric state. In addition, the residues guarding the entrance to the ligand-binding pocket of these PYLs should be bulky and hydrophobic. Based on these principles, we were able to generate monomeric PYL2 variants that gained constitutive inhibitory effect on PP2Cs. These findings provide an important framework for understanding the complex regulation of ABA signaling by PYL proteins. The Molecular Basis of ABA-Independent Inhibition of PP2Cs by a Subclass of PYL Proteins.,Hao Q, Yin P, Li W, Wang L, Yan C, Lin Z, Wu JZ, Wang J, Yan SF, Yan N Mol Cell. 2011 Jun 10;42(5):662-72. PMID:21658606[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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