3ujk: Difference between revisions

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 <StructureSection load='3ujk' size='340' side='right'caption='[[3ujk]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3ujk]] is a 1 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=3UJK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UJK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3ujk]] is a 1 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=3UJK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UJK 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></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]] 1.9&#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;'>[[3ujg|3ujg]], [[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></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABI2, At5g57050, MHM17.19 ([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/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3ujk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ujk OCA], [https://pdbe.org/3ujk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ujk RCSB], [https://www.ebi.ac.uk/pdbsum/3ujk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ujk ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/P2C77_ARATH P2C77_ARATH]] 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), high light stress, response to glucose, seed germination and inhibition of vegetative growth. During the stomatal closure regulation, modulates the inward calcium-channel permeability as well as H(2)O(2) and oxidative burst in response to ABA and dehydration. Controls negatively fibrillin that is involved in mediating ABA-induced photoprotection. May be implicated in ABA content regulation. Involved in acquired thermotolerance of root growth and seedling survival. Required for the Erwinia amylovora harpin-induced (HrpN) drought tolerance. Involved in the hydrotropic response.<ref>PMID:9165752</ref> <ref>PMID:12232276</ref> <ref>PMID:8787023</ref> <ref>PMID:9108297</ref> <ref>PMID:9090884</ref> <ref>PMID:9276963</ref> <ref>PMID:10488243</ref> <ref>PMID:10950871</ref> <ref>PMID:10872217</ref> <ref>PMID:11701885</ref> <ref>PMID:11208021</ref> <ref>PMID:11707572</ref> <ref>PMID:12194854</ref> <ref>PMID:12447533</ref> <ref>PMID:12119381</ref> <ref>PMID:14596925</ref> <ref>PMID:12609042</ref> <ref>PMID:14576281</ref> <ref>PMID:15599761</ref> <ref>PMID:15923322</ref> <ref>PMID:16339784</ref> <ref>PMID:16571665</ref> <ref>PMID:18278579</ref>
+[https://www.uniprot.org/uniprot/P2C77_ARATH P2C77_ARATH] 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), high light stress, response to glucose, seed germination and inhibition of vegetative growth. During the stomatal closure regulation, modulates the inward calcium-channel permeability as well as H(2)O(2) and oxidative burst in response to ABA and dehydration. Controls negatively fibrillin that is involved in mediating ABA-induced photoprotection. May be implicated in ABA content regulation. Involved in acquired thermotolerance of root growth and seedling survival. Required for the Erwinia amylovora harpin-induced (HrpN) drought tolerance. Involved in the hydrotropic response.<ref>PMID:9165752</ref> <ref>PMID:12232276</ref> <ref>PMID:8787023</ref> <ref>PMID:9108297</ref> <ref>PMID:9090884</ref> <ref>PMID:9276963</ref> <ref>PMID:10488243</ref> <ref>PMID:10950871</ref> <ref>PMID:10872217</ref> <ref>PMID:11701885</ref> <ref>PMID:11208021</ref> <ref>PMID:11707572</ref> <ref>PMID:12194854</ref> <ref>PMID:12447533</ref> <ref>PMID:12119381</ref> <ref>PMID:14596925</ref> <ref>PMID:12609042</ref> <ref>PMID:14576281</ref> <ref>PMID:15599761</ref> <ref>PMID:15923322</ref> <ref>PMID:16339784</ref> <ref>PMID:16571665</ref> <ref>PMID:18278579</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 3ujk" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 28: / Line 17: @@
 __TOC__
 </StructureSection>
-[[Category: Arath]]
+[[Category: Arabidopsis thaliana]]
 [[Category: Large Structures]]
-[[Category: Phosphoprotein phosphatase]]
+[[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: Abi2]]
-[[Category: Hydrolase]]
-[[Category: Protein phosphatase 2c]]