3ujg: Difference between revisions

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<StructureSection load='3ujg' size='340' side='right'caption='[[3ujg]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='3ujg' size='340' side='right'caption='[[3ujg]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ujg]] 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=3UJG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UJG FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ujg]] 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=3UJG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UJG FirstGlance]. <br>
</td></tr><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=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]] 2.6&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ujk|3ujk]], [[3ujl|3ujl]]</div></td></tr>
<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=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SRK2E, OST1, SNRK2.6, At4g33950, F17I5.140 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH]), HAB1, P2C-HA, At1g72770, F28P22.4 ([https://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'>[https://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></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=3ujg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ujg OCA], [https://pdbe.org/3ujg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ujg RCSB], [https://www.ebi.ac.uk/pdbsum/3ujg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ujg ProSAT]</span></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=3ujg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ujg OCA], [https://pdbe.org/3ujg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ujg RCSB], [https://www.ebi.ac.uk/pdbsum/3ujg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ujg ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/SRK2E_ARATH SRK2E_ARATH]] Activator of the abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomata closure in response to drought, plant pathogens, or decreases in atmospheric relative humidity (RH). Involved in the resistance to drought by avoiding water loss. Required for the stomata closure mediated by pathogen-associated molecular pattern (PAMPs) (e.g. flg22 and LPS) of pathogenic bacteria such as P.syringae pv. tomato (Pst) and E.coli O157:H7. As a plant defense process, stomata are closed transiently in order to limit invaders, but actively reopened by bacteria after a few hours; virulent strains (e.g. Pst DC3000) are more efficient than avirulent strains (e.g. Pst DC3000 AvrRpt2) in reopening stomata. Mediates the phosphorylation and activation of the S-type anion efflux channel SLAC1, and thus promotes stomata closure. Essential for stomatal closure in response to reactive oxygen species (ROS).<ref>PMID:12468729</ref> <ref>PMID:12514244</ref> <ref>PMID:12047634</ref> <ref>PMID:15064385</ref> <ref>PMID:16959575</ref> <ref>PMID:16682349</ref> <ref>PMID:16365038</ref> <ref>PMID:16766677</ref> <ref>PMID:17307925</ref> <ref>PMID:19955427</ref> <ref>PMID:19955405</ref> <ref>PMID:20128877</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/SRK2E_ARATH SRK2E_ARATH] Activator of the abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomata closure in response to drought, plant pathogens, or decreases in atmospheric relative humidity (RH). Involved in the resistance to drought by avoiding water loss. Required for the stomata closure mediated by pathogen-associated molecular pattern (PAMPs) (e.g. flg22 and LPS) of pathogenic bacteria such as P.syringae pv. tomato (Pst) and E.coli O157:H7. As a plant defense process, stomata are closed transiently in order to limit invaders, but actively reopened by bacteria after a few hours; virulent strains (e.g. Pst DC3000) are more efficient than avirulent strains (e.g. Pst DC3000 AvrRpt2) in reopening stomata. Mediates the phosphorylation and activation of the S-type anion efflux channel SLAC1, and thus promotes stomata closure. Essential for stomatal closure in response to reactive oxygen species (ROS).<ref>PMID:12468729</ref> <ref>PMID:12514244</ref> <ref>PMID:12047634</ref> <ref>PMID:15064385</ref> <ref>PMID:16959575</ref> <ref>PMID:16682349</ref> <ref>PMID:16365038</ref> <ref>PMID:16766677</ref> <ref>PMID:17307925</ref> <ref>PMID:19955427</ref> <ref>PMID:19955405</ref> <ref>PMID:20128877</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Abscisic acid (ABA) is an essential hormone for plants to survive environmental stresses. At the center of the ABA signaling network is a subfamily of type 2C protein phosphatases (PP2Cs), which form exclusive interactions with ABA receptors and subfamily 2 Snfl-related kinase (SnRK2s). Here, we report a SnRK2-PP2C complex structure, which reveals marked similarity in PP2C recognition by SnRK2 and ABA receptors. In the complex, the kinase activation loop docks into the active site of PP2C, while the conserved ABA-sensing tryptophan of PP2C inserts into the kinase catalytic cleft, thus mimicking receptor-PP2C interactions. These structural results provide a simple mechanism that directly couples ABA binding to SnRK2 kinase activation and highlight a new paradigm of kinase-phosphatase regulation through mutual packing of their catalytic sites.
 
Molecular mimicry regulates ABA signaling by SnRK2 kinases and PP2C phosphatases.,Soon FF, Ng LM, Zhou XE, West GM, Kovach A, Tan MH, Suino-Powell KM, He Y, Xu Y, Chalmers MJ, Brunzelle JS, Zhang H, Yang H, Jiang H, Li J, Yong EL, Cutler S, Zhu JK, Griffin PR, Melcher K, Xu HE Science. 2012 Jan 6;335(6064):85-8. Epub 2011 Nov 24. PMID:22116026<ref>PMID:22116026</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ujg" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Arath]]
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Brunzelle JS]]
[[Category: Brunzelle, J S]]
[[Category: He Y]]
[[Category: He, Y]]
[[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 KM]]
[[Category: Suino-Powell, K M]]
[[Category: Tan MHE]]
[[Category: Tan, M H.E]]
[[Category: Xu HE]]
[[Category: Xu, H E]]
[[Category: Xu Y]]
[[Category: Xu, Y]]
[[Category: Zhou XE]]
[[Category: Zhou, X E]]
[[Category: Aba signaling]]
[[Category: Kinase]]
[[Category: Protein phosphatase 2c]]
[[Category: Signaling protein]]
[[Category: Snrk2 6]]

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