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==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+==
<StructureSection load='4ds8' size='340' side='right' caption='[[4ds8]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
<StructureSection load='4ds8' size='340' side='right'caption='[[4ds8]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ds8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DS8 FirstGlance]. <br>
<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>
</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=GOL:GLYCEROL'>GOL</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=GOL:GLYCEROL'>GOL</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">[[3klx|3klx]], [[3oji|3oji]], [[4dsb|4dsb]], [[4dsc|4dsc]]</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=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>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At1g73000, PYL3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH]), At1g72770, HAB1 ([http://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'>[http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ds8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ds8 OCA], [http://pdbe.org/4ds8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ds8 RCSB], [http://www.ebi.ac.uk/pdbsum/4ds8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ds8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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). [[http://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/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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
*[[ABA-regulated Protein Phosphatase 2C|ABA-regulated Protein Phosphatase 2C]]
*[[Abscisic acid receptor 3D structures|Abscisic acid receptor 3D structures]]
*[[PYR/PYL/RCAR family of ABA receptors|PYR/PYL/RCAR family of ABA receptors]]
*[[Protein phosphatase 3D structures|Protein phosphatase 3D structures]]
*[[Protein phosphatase|Protein phosphatase]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Arath]]
[[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]]

Revision as of 11:36, 21 September 2022

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.
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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