4ds8: Difference between revisions

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[[Image:4ds8.jpg|left|200px]]


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==Complex structure of abscisic acid receptor PYL3-(+)-ABA-HAB1 in the presence of Mn2+==
The line below this paragraph, containing "STRUCTURE_4ds8", creates the "Structure Box" on the page.
<StructureSection load='4ds8' size='340' side='right'caption='[[4ds8]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[4ds8]] 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=4DS8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DS8 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.21&#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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
{{STRUCTURE_4ds8|  PDB=4ds8  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ds8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ds8 OCA], [https://pdbe.org/4ds8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ds8 RCSB], [https://www.ebi.ac.uk/pdbsum/4ds8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ds8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PYL3_ARATH PYL3_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;">
== Publication Abstract from PubMed ==
Abscisic acid (ABA) controls many physiological processes and mediates adaptive responses to abiotic stresses. The ABA signaling mechanisms for abscisic acid receptors PYR/PYL/RCAR (PYLs) were reported. However, it remains unclear whether the molecular mechanisms are suitable for other PYLs. Here, complex structures of PYL3 with (+)-ABA, pyrabactin and HAB1 are reported. An unexpected trans-homodimer intermediate observed in the crystal is confirmed in solution. ABA-bound PYL3 greatly promotes the generation of monomeric PYL3, which can excessively increase the efficiency of inhibiting PP2Cs. Structure-guided biochemical experiments show that Ser195 accounts for the key intermediate. Interestingly, pyrabactin binds to PYL3 in a distinct nonproductive mode with gate closure, which sheds light on the design of agonists and antagonists for abscisic acid receptors. According to different conformations of ligand-bound PYLs, the PYLs family can be divided into three subclasses, among which the trans-dimeric subclass, represented by PYL3, reveals a distinct regulatory mechanism.


===Complex structure of abscisic acid receptor PYL3-(+)-ABA-HAB1 in the presence of Mn2+===
Complex Structures of the Abscisic Acid Receptor PYL3/RCAR13 Reveal a Unique Regulatory Mechanism.,Zhang X, Zhang Q, Xin Q, Yu L, Wang Z, Wu W, Jiang L, Wang G, Tian W, Deng Z, Wang Y, Liu Z, Long J, Gong Z, Chen Z Structure. 2012 May 9;20(5):780-90. PMID:22579247<ref>PMID:22579247</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ds8" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_22579247}}, adds the Publication Abstract to the page
*[[Abscisic acid receptor 3D structures|Abscisic acid receptor 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 22579247 is the PubMed ID number.
*[[Protein phosphatase 3D structures|Protein phosphatase 3D structures]]
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== References ==
{{ABSTRACT_PUBMED_22579247}}
<references/>
 
__TOC__
==About this Structure==
</StructureSection>
[[4ds8]] 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=4DS8 OCA].
 
==Reference==
<ref group="xtra">PMID:022579247</ref><references group="xtra"/>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Phosphoprotein phosphatase]]
[[Category: Large Structures]]
[[Category: Chen, Z.]]
[[Category: Chen Z]]
[[Category: Wang, G.]]
[[Category: Wang G]]
[[Category: Zhang, Q.]]
[[Category: Zhang Q]]
[[Category: Zhang, X.]]
[[Category: Zhang X]]
[[Category: Aba]]
[[Category: Abscisic acid receptor]]
[[Category: Hormone receptor-hydrolase complex]]
[[Category: Pp2c]]
[[Category: Pyl3]]

Latest revision as of 16:44, 8 November 2023

Complex structure of abscisic acid receptor PYL3-(+)-ABA-HAB1 in the presence of Mn2+Complex structure of abscisic acid receptor PYL3-(+)-ABA-HAB1 in the presence of Mn2+

Structural highlights

4ds8 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 2.21Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PYL3_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 PubMed

Abscisic acid (ABA) controls many physiological processes and mediates adaptive responses to abiotic stresses. The ABA signaling mechanisms for abscisic acid receptors PYR/PYL/RCAR (PYLs) were reported. However, it remains unclear whether the molecular mechanisms are suitable for other PYLs. Here, complex structures of PYL3 with (+)-ABA, pyrabactin and HAB1 are reported. An unexpected trans-homodimer intermediate observed in the crystal is confirmed in solution. ABA-bound PYL3 greatly promotes the generation of monomeric PYL3, which can excessively increase the efficiency of inhibiting PP2Cs. Structure-guided biochemical experiments show that Ser195 accounts for the key intermediate. Interestingly, pyrabactin binds to PYL3 in a distinct nonproductive mode with gate closure, which sheds light on the design of agonists and antagonists for abscisic acid receptors. According to different conformations of ligand-bound PYLs, the PYLs family can be divided into three subclasses, among which the trans-dimeric subclass, represented by PYL3, reveals a distinct regulatory mechanism.

Complex Structures of the Abscisic Acid Receptor PYL3/RCAR13 Reveal a Unique Regulatory Mechanism.,Zhang X, Zhang Q, Xin Q, Yu L, Wang Z, Wu W, Jiang L, Wang G, Tian W, Deng Z, Wang Y, Liu Z, Long J, Gong Z, Chen Z Structure. 2012 May 9;20(5):780-90. PMID:22579247[1]

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

See Also

References

  1. ↑ Zhang X, Zhang Q, Xin Q, Yu L, Wang Z, Wu W, Jiang L, Wang G, Tian W, Deng Z, Wang Y, Liu Z, Long J, Gong Z, Chen Z. Complex Structures of the Abscisic Acid Receptor PYL3/RCAR13 Reveal a Unique Regulatory Mechanism. Structure. 2012 May 9;20(5):780-90. PMID:22579247 doi:10.1016/j.str.2012.02.019

4ds8, resolution 2.21Å

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