3p86

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==Crystal structure of CTR1 kinase domain mutant D676N in complex with staurosporine==
==Crystal structure of CTR1 kinase domain mutant D676N in complex with staurosporine==
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<StructureSection load='3p86' size='340' side='right' caption='[[3p86]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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<StructureSection load='3p86' size='340' side='right'caption='[[3p86]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3p86]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P86 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3P86 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3p86]] 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=3P86 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P86 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=STU:STAUROSPORINE'>STU</scene></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]] 2.496&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At5g03730, CTR1, F17C15_150 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=STU:STAUROSPORINE'>STU</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://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=3p86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p86 OCA], [https://pdbe.org/3p86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p86 RCSB], [https://www.ebi.ac.uk/pdbsum/3p86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p86 ProSAT]</span></td></tr>
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<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=3p86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p86 OCA], [http://pdbe.org/3p86 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3p86 RCSB], [http://www.ebi.ac.uk/pdbsum/3p86 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3p86 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CTR1_ARATH CTR1_ARATH]] Acts as a negative regulator in the ethylene response pathway.<ref>PMID:8431946</ref>
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[https://www.uniprot.org/uniprot/CTR1_ARATH CTR1_ARATH] Acts as a negative regulator in the ethylene response pathway.<ref>PMID:8431946</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Ethylene controls many aspects of plant growth and development. Signaling by the gaseous phytohormone is initiated by disulfide-linked membrane-bound receptors, and the formation of heteromeric receptor clusters contributes to the broad range of ethylene responsiveness. In Arabidopsis thaliana, the TCS-like ethylene receptors interact with the cytosolic serine/threonine kinase constitutive triple response 1 (CTR1), a proposed mitogen-activated protein kinase kinase kinase. In the absence of the hormone, the receptor and therefore CTR1 are active. Hence, ethylene acts as an inverse agonist of its signaling pathway. The three-dimensional structures of the active, triphosphorylated and the unphosphorylated, inactive kinase domain of CTR1 in complex with staurosporine illustrate the conformational rearrangements that form the basis of activity regulation. Additionally, in analytical ultracentrifugation experiments, active kinase domains form back-to-back dimers, while inactive and activation loop variants are monomers. Together with a front-to-front activation interface, the active protein kinase dimers thereby engage in interactions that promote CTR1-mediated cross talk between ethylene receptor clusters. This model provides a structural foundation for the observed high sensitivity of plants to ethylene.
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Protein kinase domain of CTR1 from Arabidopsis thaliana promotes ethylene receptor cross talk.,Mayerhofer H, Panneerselvam S, Mueller-Dieckmann J J Mol Biol. 2012 Jan 27;415(4):768-79. Epub 2011 Dec 7. PMID:22155294<ref>PMID:22155294</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 3p86" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Serine/threonine protein kinase|Serine/threonine protein kinase]]
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*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arath]]
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[[Category: Arabidopsis thaliana]]
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[[Category: Non-specific serine/threonine protein kinase]]
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[[Category: Large Structures]]
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[[Category: Mayerhofer, H]]
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[[Category: Mayerhofer H]]
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[[Category: Mueller-Dieckmann, J]]
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[[Category: Mueller-Dieckmann J]]
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[[Category: Panneerselvam, S]]
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[[Category: Panneerselvam S]]
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[[Category: Ers1]]
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[[Category: Etr1]]
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[[Category: Etr2]]
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[[Category: Kinase]]
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[[Category: Phosphorylation]]
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[[Category: Transferase]]
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Current revision

Crystal structure of CTR1 kinase domain mutant D676N in complex with staurosporine

PDB ID 3p86

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