2c7y

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[[Image:2c7y.gif|left|200px]]
 
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{{Structure
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==plant enzyme==
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|PDB= 2c7y |SIZE=350|CAPTION= <scene name='initialview01'>2c7y</scene>, resolution 2.10&Aring;
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<StructureSection load='2c7y' size='340' side='right'caption='[[2c7y]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[2c7y]] 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=2C7Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C7Y FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_C-acyltransferase Acetyl-CoA C-acyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.16 2.3.1.16] </span>
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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]] 2.1&#8491;</td></tr>
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|GENE=
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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=2c7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c7y OCA], [https://pdbe.org/2c7y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c7y RCSB], [https://www.ebi.ac.uk/pdbsum/2c7y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c7y ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c7y OCA], [http://www.ebi.ac.uk/pdbsum/2c7y PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c7y RCSB]</span>
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[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>
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c7/2c7y_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2c7y ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Crystal structures of peroxisomal Arabidopsis thaliana 3-ketoacyl-CoA thiolase (AtKAT), an enzyme of fatty acid beta-oxidation, are reported. The subunit, a typical thiolase, is a combination of two similar alpha/beta domains capped with a loop domain. The comparison of AtKAT with the Saccharomyces cerevisiae homologue (ScKAT) structure reveals a different placement of subunits within the functional dimers and that a polypeptide segment forming an extended loop around the open catalytic pocket of ScKAT converts to alpha-helix in AtKAT, and occludes the active site. A disulfide is formed between Cys192, on this helix, and Cys138, a catalytic residue. Access to Cys138 is determined by the structure of this polypeptide segment. AtKAT represents an oxidized, previously unknown inactive form, whilst ScKAT is the reduced and active enzyme. A high level of sequence conservation is observed, including Cys192, in eukaryotic peroxisomal, but not mitochondrial or prokaryotic KAT sequences, for this labile loop/helix segment. This indicates that KAT activity in peroxisomes is influenced by a disulfide/dithiol change linking fatty acid beta-oxidation with redox regulation.
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'''PLANT ENZYME'''
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The crystal structure of a plant 3-ketoacyl-CoA thiolase reveals the potential for redox control of peroxisomal fatty acid beta-oxidation.,Sundaramoorthy R, Micossi E, Alphey MS, Germain V, Bryce JH, Smith SM, Leonard GA, Hunter WN J Mol Biol. 2006 Jun 2;359(2):347-57. Epub 2006 Mar 29. PMID:16630629<ref>PMID:16630629</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 2c7y" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Crystal structures of peroxisomal Arabidopsis thaliana 3-ketoacyl-CoA thiolase (AtKAT), an enzyme of fatty acid beta-oxidation, are reported. The subunit, a typical thiolase, is a combination of two similar alpha/beta domains capped with a loop domain. The comparison of AtKAT with the Saccharomyces cerevisiae homologue (ScKAT) structure reveals a different placement of subunits within the functional dimers and that a polypeptide segment forming an extended loop around the open catalytic pocket of ScKAT converts to alpha-helix in AtKAT, and occludes the active site. A disulfide is formed between Cys192, on this helix, and Cys138, a catalytic residue. Access to Cys138 is determined by the structure of this polypeptide segment. AtKAT represents an oxidized, previously unknown inactive form, whilst ScKAT is the reduced and active enzyme. A high level of sequence conservation is observed, including Cys192, in eukaryotic peroxisomal, but not mitochondrial or prokaryotic KAT sequences, for this labile loop/helix segment. This indicates that KAT activity in peroxisomes is influenced by a disulfide/dithiol change linking fatty acid beta-oxidation with redox regulation.
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*[[Thiolase 3D structures|Thiolase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2C7Y is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C7Y OCA].
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__TOC__
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</StructureSection>
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==Reference==
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The crystal structure of a plant 3-ketoacyl-CoA thiolase reveals the potential for redox control of peroxisomal fatty acid beta-oxidation., Sundaramoorthy R, Micossi E, Alphey MS, Germain V, Bryce JH, Smith SM, Leonard GA, Hunter WN, J Mol Biol. 2006 Jun 2;359(2):347-57. Epub 2006 Mar 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16630629 16630629]
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[[Category: Acetyl-CoA C-acyltransferase]]
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[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Alphey, M S.]]
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[[Category: Alphey MS]]
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[[Category: Bryce, J H.]]
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[[Category: Bryce JH]]
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[[Category: Germain, V.]]
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[[Category: Germain V]]
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[[Category: Hunter, W N.]]
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[[Category: Hunter WN]]
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[[Category: Leonard, G A.]]
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[[Category: Leonard GA]]
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[[Category: Micossi, E.]]
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[[Category: Micossi E]]
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[[Category: Smith, S M.]]
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[[Category: Smith SM]]
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[[Category: Sundaramoorthy, R.]]
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[[Category: Sundaramoorthy R]]
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[[Category: 3-ketoacylcoa thiolase]]
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[[Category: acyltransferase]]
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[[Category: fatty acid metabolism]]
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[[Category: lipid synthesis]]
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[[Category: oxylipin synthesis]]
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[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:17:41 2008''
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Current revision

plant enzyme

PDB ID 2c7y

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