3uc4

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<StructureSection load='3uc4' size='340' side='right'caption='[[3uc4]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3uc4' size='340' side='right'caption='[[3uc4]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3uc4]] 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=3UC4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UC4 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3uc4]] 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=3UC4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UC4 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3uc3|3uc3]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<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])</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3uc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uc4 OCA], [https://pdbe.org/3uc4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uc4 RCSB], [https://www.ebi.ac.uk/pdbsum/3uc4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uc4 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=3uc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uc4 OCA], [https://pdbe.org/3uc4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uc4 RCSB], [https://www.ebi.ac.uk/pdbsum/3uc4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uc4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Abscisic acid (ABA) is an essential hormone that controls plant growth, development, and responses to abiotic stresses. Central for ABA signaling is the ABA-mediated autoactivation of three monomeric Snf1-related kinases (SnRK2.2, -2.3, and -2.6). In the absence of ABA, SnRK2s are kept in an inactive state by forming physical complexes with type 2C protein phosphatases (PP2Cs). Upon relief of this inhibition, SnRK2 kinases can autoactivate through unknown mechanisms. Here, we report the crystal structures of full-length Arabidopsis thaliana SnRK2.3 and SnRK2.6 at 1.9- and 2.3-A resolution, respectively. The structures, in combination with biochemical studies, reveal a two-step mechanism of intramolecular kinase activation that resembles the intermolecular activation of cyclin-dependent kinases. First, release of inhibition by PP2C allows the SnRK2s to become partially active because of an intramolecular stabilization of the catalytic domain by a conserved helix in the kinase regulatory domain. This stabilization enables SnRK2s to gain full activity by activation loop autophosphorylation. Autophosphorylation is more efficient in SnRK2.6, which has higher stability than SnRK2.3 and has well-structured activation loop phosphate acceptor sites that are positioned next to the catalytic site. Together, these data provide a structural framework that links ABA-mediated release of PP2C inhibition to activation of SnRK2 kinases.
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Structural basis for basal activity and autoactivation of abscisic acid (ABA) signaling SnRK2 kinases.,Ng LM, Soon FF, Zhou XE, West GM, Kovach A, Suino-Powell KM, Chalmers MJ, Li J, Yong EL, Zhu JK, Griffin PR, Melcher K, Xu HE Proc Natl Acad Sci U S A. 2011 Dec 27;108(52):21259-64. Epub 2011 Dec 12. PMID:22160701<ref>PMID:22160701</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3uc4" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arath]]
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[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Non-specific serine/threonine protein kinase]]
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[[Category: Kovach A]]
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[[Category: Kovach, A]]
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[[Category: Li J]]
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[[Category: Li, J]]
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[[Category: Melcher K]]
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[[Category: Melcher, K]]
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[[Category: Ng L-M]]
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[[Category: Ng, L M]]
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[[Category: Soon F-F]]
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[[Category: Soon, F F]]
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[[Category: Suino-Powell KM]]
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[[Category: Suino-Powell, K M]]
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[[Category: Xu HE]]
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[[Category: Xu, H E]]
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[[Category: Zhou XE]]
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[[Category: Zhou, X E]]
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[[Category: Aba signaling]]
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[[Category: Kinase]]
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[[Category: Snrk2 6]]
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[[Category: Transferase]]
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Current revision

The crystal structure of Snf1-related kinase 2.6

PDB ID 3uc4

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