3qn1: Difference between revisions
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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]] 1.80Å' scene=''> | <StructureSection load='3qn1' size='340' side='right'caption='[[3qn1]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3qn1]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3qn1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. 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='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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3k90|3k90]], [[3k3k|3k3k]], [[3nmt|3nmt]], [[3njo|3njo]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABIP6, At4g17870, PYR1, RCAR11, T6K21.50 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABIP6, At4g17870, PYR1, RCAR11, T6K21.50 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH]), At1g72770, F28P22.4, HAB1, P2C-HA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [https://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'>[ | <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> | ||
</table> | </table> | ||
== Function == | == 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> [[https://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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[ | *[[Abscisic acid receptor 3D structures|Abscisic acid receptor 3D structures]] | ||
*[[Protein phosphatase 3D structures|Protein phosphatase 3D structures]] | |||
*[[Protein phosphatase|Protein phosphatase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Arath]] | [[Category: Arath]] | ||
[[Category: Large Structures]] | |||
[[Category: Phosphoprotein phosphatase]] | [[Category: Phosphoprotein phosphatase]] | ||
[[Category: Betz, K]] | [[Category: Betz, K]] |
Revision as of 09:15, 8 June 2022
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
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] [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.[4] [5] [6] [7] Publication Abstract from PubMedThe 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[8] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Arath
- Large Structures
- Phosphoprotein phosphatase
- Betz, K
- Dupeux, F
- Marquez, J A
- Santiago, J
- Abiotic stress
- Abscisic acid binding
- Abscisic acid hormone receptor
- Bet v domain
- Intracellular
- Nucleus
- Plant stress response
- Pp2c
- Protein binding
- Pyr/pyl/rcar
- Start domain
- Type 2c protein phosphatase
- Type 2c protein phosphatase binding