3nmn: Difference between revisions

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{{STRUCTURE_3nmn|  PDB=3nmn  |  SCENE=  }}
==Crystal structure of pyrabactin-bound abscisic acid receptor PYL1 in complex with type 2C protein phosphatase ABI1==
===Crystal structure of pyrabactin-bound abscisic acid receptor PYL1 in complex with type 2C protein phosphatase ABI1===
<StructureSection load='3nmn' size='340' side='right' caption='[[3nmn]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
{{ABSTRACT_PUBMED_20729862}}
== Structural highlights ==
<table><tr><td colspan='2'>[[3nmn]] is a 4 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=3NMN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NMN FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PYV:4-BROMO-N-(PYRIDIN-2-YLMETHYL)NAPHTHALENE-1-SULFONAMIDE'>PYV</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kay|3kay]], [[3nmh|3nmh]], [[3nmp|3nmp]], [[3nmt|3nmt]], [[3nmv|3nmv]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PYL1, RCAR12, At5g46790, MZA15.21 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana]), ABI1, At4g26080, F20B18.190 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])</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=3nmn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nmn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nmn RCSB], [http://www.ebi.ac.uk/pdbsum/3nmn PDBsum]</span></td></tr>
</table>
== 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/3nmn_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/chain_selection.php?pdb_ID=2ata 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.


==Function==
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>
[[http://www.uniprot.org/uniprot/PYL1_ARATH PYL1_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:19407143</ref> <ref>PMID:19898420</ref> <ref>PMID:19855379</ref> <ref>PMID:19893533</ref>  [[http://www.uniprot.org/uniprot/P2C56_ARATH P2C56_ARATH]] Key component and repressor of the abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomatal closure, osmotic water permeability of the plasma membrane (Pos), drought-induced resistance and rhizogenesis, response to glucose, high light stress, seed germination and inhibition of vegetative growth. During the stomatal closure regulation, modulates the inward calcium-channel permeability as well as the actin reorganization in guard cells in response to ABA. Involved in the resistance to the bacterial pathogen Pseudomonas syringae pv. tomato. Controls negatively fibrillin expression that is involved in mediating ABA-induced photoprotection. May be involved in ABA content regulation. Plays a role in the Pro accumulation in response to reduced water availability (low water potential). Required for the ABA negative regulation of the ethylene-induced hyponastic growth. Involved in acquired thermotolerance of root growth and seedling survival. Activates/represses SRK2E/OST1 in response to ABA-dependent stimuli, especially in stomata closure regulation involving SLAC1.<ref>PMID:12228349</ref> <ref>PMID:1834244</ref> <ref>PMID:16652949</ref> <ref>PMID:8492808</ref> <ref>PMID:12232276</ref> <ref>PMID:12232124</ref> <ref>PMID:7568166</ref> <ref>PMID:12228349</ref> <ref>PMID:8898906</ref> <ref>PMID:8771791</ref> <ref>PMID:9108297</ref> <ref>PMID:9090884</ref> <ref>PMID:9165752</ref> <ref>PMID:9161030</ref> <ref>PMID:9263461</ref> <ref>PMID:9351242</ref> <ref>PMID:9276963</ref> <ref>PMID:9448270</ref> <ref>PMID:10645425</ref> <ref>PMID:10488243</ref> <ref>PMID:10521520</ref> <ref>PMID:10950871</ref> <ref>PMID:10872217</ref> <ref>PMID:11707572</ref> <ref>PMID:11208021</ref> <ref>PMID:11587514</ref> <ref>PMID:11289613</ref> <ref>PMID:11701885</ref> <ref>PMID:12194854</ref> <ref>PMID:12065416</ref> <ref>PMID:12432076</ref> <ref>PMID:12047634</ref> <ref>PMID:12713537</ref> <ref>PMID:14576281</ref> <ref>PMID:14596925</ref> <ref>PMID:12609042</ref> <ref>PMID:15144382</ref> <ref>PMID:15197253</ref> <ref>PMID:15618419</ref> <ref>PMID:15923322</ref> <ref>PMID:16365038</ref> <ref>PMID:16339784</ref> <ref>PMID:16571665</ref> <ref>PMID:16798945</ref> <ref>PMID:16614222</ref> <ref>PMID:17304219</ref> <ref>PMID:17158582</ref> <ref>PMID:18298671</ref> <ref>PMID:19955405</ref>


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[3nmn]] is a 4 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=3NMN OCA].
</div>


==See Also==
==See Also==
*[[ABA-regulated Protein Phosphatase 2C|ABA-regulated Protein Phosphatase 2C]]
*[[PYR/PYL/RCAR family of ABA receptors|PYR/PYL/RCAR family of ABA receptors]]
*[[Protein phosphatase|Protein phosphatase]]
*[[Protein phosphatase|Protein phosphatase]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:020729862</ref><references group="xtra"/><references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Phosphoprotein phosphatase]]
[[Category: Phosphoprotein phosphatase]]
[[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, K M]]
[[Category: Xu, H E.]]
[[Category: Xu, H E]]
[[Category: Xu, Y.]]
[[Category: Xu, Y]]
[[Category: Yong, E L.]]
[[Category: Yong, E L]]
[[Category: Zhou, X E.]]
[[Category: Zhou, X E]]
[[Category: Abscisic acid signaling]]
[[Category: Abscisic acid signaling]]
[[Category: Plant hormone receptor]]
[[Category: Plant hormone receptor]]

Revision as of 10:19, 19 December 2014

Crystal structure of pyrabactin-bound abscisic acid receptor PYL1 in complex with type 2C protein phosphatase ABI1Crystal structure of pyrabactin-bound abscisic acid receptor PYL1 in complex with type 2C protein phosphatase ABI1

Structural highlights

3nmn is a 4 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:,
Gene:PYL1, RCAR12, At5g46790, MZA15.21 (Arabidopsis thaliana), ABI1, At4g26080, F20B18.190 (Arabidopsis thaliana)
Activity:Phosphoprotein phosphatase, with EC number 3.1.3.16
Resources:FirstGlance, OCA, RCSB, PDBsum

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[1]

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

See Also

References

  1. ↑ 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

3nmn, resolution 2.15Å

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