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{{Seed}}
[[Image:3nmt.jpg|left|200px]]


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==Crystal structure of pyrabactin bound abscisic acid receptor PYL2 mutant A93F in complex with type 2C protein phosphatase HAB1==
The line below this paragraph, containing "STRUCTURE_3nmt", creates the "Structure Box" on the page.
<StructureSection load='3nmt' size='340' side='right'caption='[[3nmt]], [[Resolution|resolution]] 2.56&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'>[[3nmt]] 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=3NMT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NMT 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]] 2.56&#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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PYV:4-BROMO-N-(PYRIDIN-2-YLMETHYL)NAPHTHALENE-1-SULFONAMIDE'>PYV</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
{{STRUCTURE_3nmt|  PDB=3nmt  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3nmt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nmt OCA], [https://pdbe.org/3nmt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nmt RCSB], [https://www.ebi.ac.uk/pdbsum/3nmt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nmt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PYL2_ARATH PYL2_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:19898420</ref> <ref>PMID:19893533</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nm/3nmt_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3nmt ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The phytohormone abscisic acid (ABA) functions through a family of fourteen PYR/PYL receptors, which were identified by resistance to pyrabactin, a synthetic inhibitor of seed germination. ABA activates these receptors to inhibit type 2C protein phosphatases, such as ABI1, yet it remains unclear whether these receptors can be antagonized. Here we demonstrate that pyrabactin is an agonist of PYR1 and PYL1 but is unexpectedly an antagonist of PYL2. Crystal structures of the PYL2-pyrabactin and PYL1-pyrabactin-ABI1 complexes reveal the mechanism responsible for receptor-selective activation and inhibition, which enables us to design mutations that convert PYL1 to a pyrabactin-inhibited receptor and PYL2 to a pyrabactin-activated receptor and to identify new pyrabactin-based ABA receptor agonists. Together, our results establish a new concept of ABA receptor antagonism, illustrate its underlying mechanisms and provide a rational framework for discovering novel ABA receptor ligands.


===Crystal structure of pyrabactin bound abscisic acid receptor PYL2 mutant A93F in complex with type 2C protein phosphatase HAB1===
Identification and mechanism of ABA receptor antagonism.,Melcher K, Xu Y, Ng LM, Zhou XE, Soon FF, Chinnusamy V, Suino-Powell KM, Kovach A, Tham FS, Cutler SR, Li J, Yong EL, Zhu JK, Xu HE Nat Struct Mol Biol. 2010 Sep;17(9):1102-8. Epub 2010 Aug 22. PMID:20729862<ref>PMID:20729862</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3nmt" style="background-color:#fffaf0;"></div>


==About this Structure==
==See Also==
3NMT is a 2 chains structure with sequences 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=3NMT OCA].
*[[Abscisic acid receptor 3D structures|Abscisic acid receptor 3D structures]]
*[[Protein phosphatase 3D structures|Protein phosphatase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Phosphoprotein phosphatase]]
[[Category: Large Structures]]
[[Category: Kovach, A.]]
[[Category: Kovach A]]
[[Category: Li, J.]]
[[Category: Li J]]
[[Category: Melcher, K.]]
[[Category: Melcher K]]
[[Category: Ng, L M.]]
[[Category: Ng L-M]]
[[Category: Soon, F F.]]
[[Category: Soon F-F]]
[[Category: Suino-Powell, K M.]]
[[Category: Suino-Powell KM]]
[[Category: Xu, H E.]]
[[Category: Xu HE]]
[[Category: Xu, Y.]]
[[Category: Xu Y]]
[[Category: Yong, E L.]]
[[Category: Yong E-L]]
[[Category: Zhou, X E.]]
[[Category: Zhou XE]]
[[Category: Abscisic acid receptor]]
[[Category: Helix-grip fold]]
[[Category: Protein binding]]
[[Category: Pyl2]]
[[Category: Pyrabactin]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 25 09:00:24 2010''

Latest revision as of 12:17, 6 September 2023

Crystal structure of pyrabactin bound abscisic acid receptor PYL2 mutant A93F in complex with type 2C protein phosphatase HAB1Crystal structure of pyrabactin bound abscisic acid receptor PYL2 mutant A93F in complex with type 2C protein phosphatase HAB1

Structural highlights

3nmt 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 2.56Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PYL2_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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The phytohormone abscisic acid (ABA) functions through a family of fourteen PYR/PYL receptors, which were identified by resistance to pyrabactin, a synthetic inhibitor of seed germination. ABA activates these receptors to inhibit type 2C protein phosphatases, such as ABI1, yet it remains unclear whether these receptors can be antagonized. Here we demonstrate that pyrabactin is an agonist of PYR1 and PYL1 but is unexpectedly an antagonist of PYL2. Crystal structures of the PYL2-pyrabactin and PYL1-pyrabactin-ABI1 complexes reveal the mechanism responsible for receptor-selective activation and inhibition, which enables us to design mutations that convert PYL1 to a pyrabactin-inhibited receptor and PYL2 to a pyrabactin-activated receptor and to identify new pyrabactin-based ABA receptor agonists. Together, our results establish a new concept of ABA receptor antagonism, illustrate its underlying mechanisms and provide a rational framework for discovering novel ABA receptor ligands.

Identification and mechanism of ABA receptor antagonism.,Melcher K, Xu Y, Ng LM, Zhou XE, Soon FF, Chinnusamy V, Suino-Powell KM, Kovach A, Tham FS, Cutler SR, Li J, Yong EL, Zhu JK, Xu HE Nat Struct Mol Biol. 2010 Sep;17(9):1102-8. Epub 2010 Aug 22. PMID:20729862[3]

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

See Also

References

  1. ↑ Melcher K, Ng LM, Zhou XE, Soon FF, Xu Y, Suino-Powell KM, Park SY, Weiner JJ, Fujii H, Chinnusamy V, Kovach A, Li J, Wang Y, Li J, Peterson FC, Jensen DR, Yong EL, Volkman BF, Cutler SR, Zhu JK, Xu HE. A gate-latch-lock mechanism for hormone signalling by abscisic acid receptors. Nature. 2009 Dec 3;462(7273):602-8. PMID:19898420 doi:10.1038/nature08613
  2. ↑ Yin P, Fan H, Hao Q, Yuan X, Wu D, Pang Y, Yan C, Li W, Wang J, Yan N. Structural insights into the mechanism of abscisic acid signaling by PYL proteins. Nat Struct Mol Biol. 2009 Dec;16(12):1230-6. Epub 2009 Nov 5. PMID:19893533 doi:10.1038/nsmb.1730
  3. ↑ Melcher K, Xu Y, Ng LM, Zhou XE, Soon FF, Chinnusamy V, Suino-Powell KM, Kovach A, Tham FS, Cutler SR, Li J, Yong EL, Zhu JK, Xu HE. Identification and mechanism of ABA receptor antagonism. Nat Struct Mol Biol. 2010 Sep;17(9):1102-8. Epub 2010 Aug 22. PMID:20729862 doi:10.1038/nsmb.1887

3nmt, resolution 2.56Å

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