3zvu: Difference between revisions

Latest revision as of 11:14, 20 December 2023

Structure of the PYR1 His60Pro mutant in complex with the HAB1 phosphatase and Abscisic acid

Structural highlights

3zvu is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.1Å
Ligands:	A8S, MN, SO4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

Publication Abstract from PubMed

Abscisic acid (ABA) is a key hormone regulating plant growth, development and the response to biotic and abiotic stress. ABA binding to pyrabactin resistance (PYR)/PYR1-like (PYL)/Regulatory Component of Abscisic acid Receptor (RCAR) intracellular receptors promotes the formation of stable complexes with certain protein phosphatases type 2C (PP2Cs), leading to the activation of ABA signalling. The PYR/PYL/RCAR family contains 14 genes in Arabidopsis and is currently the largest plant hormone receptor family known; however, it is unclear what functional differentiation exists among receptors. Here, we identify two distinct classes of receptors, dimeric and monomeric, with different intrinsic affinities for ABA and whose differential properties are determined by the oligomeric state of their apo forms. Moreover, we find a residue in PYR1, H60, that is variable between family members and plays a key role in determining oligomeric state. In silico modelling of the ABA activation pathway reveals that monomeric receptors have a competitive advantage for binding to ABA and PP2Cs. This work illustrates how receptor oligomerization can modulate hormonal responses and more generally, the sensitivity of a ligand-dependent signalling system.

A thermodynamic switch modulates abscisic acid receptor sensitivity.,Dupeux F, Santiago J, Betz K, Twycross J, Park SY, Rodriguez L, Gonzalez-Guzman M, Jensen MR, Krasnogor N, Blackledge M, Holdsworth M, Cutler SR, Rodriguez PL, Marquez JA EMBO J. 2011 Aug 16;30(20):4171-84. doi: 10.1038/emboj.2011.294. PMID:21847091^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Santiago J, Rodrigues A, Saez A, Rubio S, Antoni R, Dupeux F, Park SY, Marquez JA, Cutler SR, Rodriguez PL. Modulation of drought resistance by the abscisic acid receptor PYL5 through inhibition of clade A PP2Cs. Plant J. 2009 Nov;60(4):575-88. doi: 10.1111/j.1365-313X.2009.03981.x. Epub 2009 , Jul 16. PMID:19624469 doi:10.1111/j.1365-313X.2009.03981.x
↑ Park SY, Fung P, Nishimura N, Jensen DR, Fujii H, Zhao Y, Lumba S, Santiago J, Rodrigues A, Chow TF, Alfred SE, Bonetta D, Finkelstein R, Provart NJ, Desveaux D, Rodriguez PL, McCourt P, Zhu JK, Schroeder JI, Volkman BF, Cutler SR. Abscisic acid inhibits type 2C protein phosphatases via the PYR/PYL family of START proteins. Science. 2009 May 22;324(5930):1068-71. doi: 10.1126/science.1173041. Epub 2009, Apr 30. PMID:19407142 doi:10.1126/science.1173041
↑ Szostkiewicz I, Richter K, Kepka M, Demmel S, Ma Y, Korte A, Assaad FF, Christmann A, Grill E. Closely related receptor complexes differ in their ABA selectivity and sensitivity. Plant J. 2010 Jan;61(1):25-35. doi: 10.1111/j.1365-313X.2009.04025.x. Epub 2009, Sep 21. PMID:19769575 doi:10.1111/j.1365-313X.2009.04025.x
↑ Dupeux F, Santiago J, Betz K, Twycross J, Park SY, Rodriguez L, Gonzalez-Guzman M, Jensen MR, Krasnogor N, Blackledge M, Holdsworth M, Cutler SR, Rodriguez PL, Marquez JA. A thermodynamic switch modulates abscisic acid receptor sensitivity. EMBO J. 2011 Aug 16;30(20):4171-84. doi: 10.1038/emboj.2011.294. PMID:21847091 doi:10.1038/emboj.2011.294

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Santiago J, Rodrigues A, Saez A, Rubio S, Antoni R, Dupeux F, Park SY, Marquez JA, Cutler SR, Rodriguez PL. Modulation of drought resistance by the abscisic acid receptor PYL5 through inhibition of clade A PP2Cs. Plant J. 2009 Nov;60(4):575-88. doi: 10.1111/j.1365-313X.2009.03981.x. Epub 2009 , Jul 16. PMID:19624469 doi:10.1111/j.1365-313X.2009.03981.x

[2] Park SY, Fung P, Nishimura N, Jensen DR, Fujii H, Zhao Y, Lumba S, Santiago J, Rodrigues A, Chow TF, Alfred SE, Bonetta D, Finkelstein R, Provart NJ, Desveaux D, Rodriguez PL, McCourt P, Zhu JK, Schroeder JI, Volkman BF, Cutler SR. Abscisic acid inhibits type 2C protein phosphatases via the PYR/PYL family of START proteins. Science. 2009 May 22;324(5930):1068-71. doi: 10.1126/science.1173041. Epub 2009, Apr 30. PMID:19407142 doi:10.1126/science.1173041

[3] Szostkiewicz I, Richter K, Kepka M, Demmel S, Ma Y, Korte A, Assaad FF, Christmann A, Grill E. Closely related receptor complexes differ in their ABA selectivity and sensitivity. Plant J. 2010 Jan;61(1):25-35. doi: 10.1111/j.1365-313X.2009.04025.x. Epub 2009, Sep 21. PMID:19769575 doi:10.1111/j.1365-313X.2009.04025.x

[4] Dupeux F, Santiago J, Betz K, Twycross J, Park SY, Rodriguez L, Gonzalez-Guzman M, Jensen MR, Krasnogor N, Blackledge M, Holdsworth M, Cutler SR, Rodriguez PL, Marquez JA. A thermodynamic switch modulates abscisic acid receptor sensitivity. EMBO J. 2011 Aug 16;30(20):4171-84. doi: 10.1038/emboj.2011.294. PMID:21847091 doi:10.1038/emboj.2011.294

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[2]

[3]

[4]

@@ Line 3: / Line 3: @@
 <StructureSection load='3zvu' size='340' side='right'caption='[[3zvu]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3zvu]] 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=3ZVU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZVU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3zvu]] 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=3ZVU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZVU FirstGlance]. <br>
-</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</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>
-<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='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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3zvu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zvu OCA], [https://pdbe.org/3zvu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zvu RCSB], [https://www.ebi.ac.uk/pdbsum/3zvu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zvu 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>  [[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>
+[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 27: / Line 27: @@
 __TOC__
 </StructureSection>
-[[Category: Arath]]
+[[Category: Arabidopsis thaliana]]
 [[Category: Large Structures]]
-[[Category: Phosphoprotein phosphatase]]
+[[Category: Betz K]]
-[[Category: Betz, K]]
+[[Category: Dupeux F]]
-[[Category: Dupeux, F]]
+[[Category: Marquez JA]]
-[[Category: Marquez, J A]]
+[[Category: Rodriguez PL]]
-[[Category: Rodriguez, P L]]
+[[Category: Santiago J]]
-[[Category: Santiago, J]]
-[[Category: Hormone receptor]]
-[[Category: Receptor-hydrolase complex]]
-[[Category: Stress response]]

3zvu: Difference between revisions

Latest revision as of 11:14, 20 December 2023

Structure of the PYR1 His60Pro mutant in complex with the HAB1 phosphatase and Abscisic acid

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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