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< | ==Crystal structure of peroxisomal KAT2 from Arabidopsis thaliana== | ||
<StructureSection load='2wu9' size='340' side='right'caption='[[2wu9]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2wu9]] 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=2WU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WU9 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></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=2wu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wu9 OCA], [https://pdbe.org/2wu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wu9 RCSB], [https://www.ebi.ac.uk/pdbsum/2wu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wu9 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/THIK2_ARATH THIK2_ARATH] Involved in long chain fatty-acid beta-oxidation prior to gluconeogenesis during germination and subsequent seedling growth. Confers sensitivity to 2,4-dichlorophenoxybutiric acid (2,4-DB). Required for local and systemic induction of jasmonic acid (JA) biosynthesis after wounding. Seems to be involved in JA biosynthesis during senescence.<ref>PMID:9490742</ref> <ref>PMID:11696182</ref> <ref>PMID:11891244</ref> <ref>PMID:15141068</ref> <ref>PMID:15979881</ref> | |||
== 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/wu/2wu9_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/main_output.php?pdb_ID=2wu9 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The breakdown of fatty acids, performed by the beta-oxidation cycle, is crucial for plant germination and sustainability. beta-Oxidation involves four enzymatic reactions. The final step, in which a two-carbon unit is cleaved from the fatty acid, is performed by a 3-ketoacyl-CoA thiolase (KAT). The shortened fatty acid may then pass through the cycle again (until reaching acetoacetyl-CoA) or be directed to a different cellular function. Crystal structures of KAT from Arabidopsis thaliana and Helianthus annuus have been solved to 1.5 and 1.8 A resolution, respectively. Their dimeric structures are very similar and exhibit a typical thiolase-like fold; dimer formation and active site conformation appear in an open, active, reduced state. Using an interdisciplinary approach, we confirmed the potential of plant KATs to be regulated by the redox environment in the peroxisome within a physiological range. In addition, co-immunoprecipitation studies suggest an interaction between KAT and the multifunctional protein that is responsible for the preceding two steps in beta-oxidation, which would allow a route for substrate channeling. We suggest a model for this complex based on the bacterial system. | |||
Peroxisomal plant 3-ketoacyl-CoA thiolase structure and activity are regulated by a sensitive redox switch.,Pye VE, Christensen CE, Dyer JH, Arent S, Henriksen A J Biol Chem. 2010 Jul 30;285(31):24078-88. Epub 2010 May 12. PMID:20463027<ref>PMID:20463027</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2wu9" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Thiolase 3D structures|Thiolase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
== | |||
< | |||
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: Arent | [[Category: Large Structures]] | ||
[[Category: Christensen | [[Category: Arent S]] | ||
[[Category: Dyer | [[Category: Christensen CE]] | ||
[[Category: Henriksen | [[Category: Dyer JH]] | ||
[[Category: Pye | [[Category: Henriksen A]] | ||
[[Category: Pye VE]] | |||
Latest revision as of 13:16, 20 December 2023
Crystal structure of peroxisomal KAT2 from Arabidopsis thalianaCrystal structure of peroxisomal KAT2 from Arabidopsis thaliana
Structural highlights
FunctionTHIK2_ARATH Involved in long chain fatty-acid beta-oxidation prior to gluconeogenesis during germination and subsequent seedling growth. Confers sensitivity to 2,4-dichlorophenoxybutiric acid (2,4-DB). Required for local and systemic induction of jasmonic acid (JA) biosynthesis after wounding. Seems to be involved in JA biosynthesis during senescence.[1] [2] [3] [4] [5] 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 PubMedThe breakdown of fatty acids, performed by the beta-oxidation cycle, is crucial for plant germination and sustainability. beta-Oxidation involves four enzymatic reactions. The final step, in which a two-carbon unit is cleaved from the fatty acid, is performed by a 3-ketoacyl-CoA thiolase (KAT). The shortened fatty acid may then pass through the cycle again (until reaching acetoacetyl-CoA) or be directed to a different cellular function. Crystal structures of KAT from Arabidopsis thaliana and Helianthus annuus have been solved to 1.5 and 1.8 A resolution, respectively. Their dimeric structures are very similar and exhibit a typical thiolase-like fold; dimer formation and active site conformation appear in an open, active, reduced state. Using an interdisciplinary approach, we confirmed the potential of plant KATs to be regulated by the redox environment in the peroxisome within a physiological range. In addition, co-immunoprecipitation studies suggest an interaction between KAT and the multifunctional protein that is responsible for the preceding two steps in beta-oxidation, which would allow a route for substrate channeling. We suggest a model for this complex based on the bacterial system. Peroxisomal plant 3-ketoacyl-CoA thiolase structure and activity are regulated by a sensitive redox switch.,Pye VE, Christensen CE, Dyer JH, Arent S, Henriksen A J Biol Chem. 2010 Jul 30;285(31):24078-88. Epub 2010 May 12. PMID:20463027[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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