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2c7z

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(New page: 200px<br /><applet load="2c7z" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c7z, resolution 2.37&Aring;" /> '''PLANT ENZYME CRYSTAL...)
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[[Image:2c7z.gif|left|200px]]<br /><applet load="2c7z" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2c7z, resolution 2.37&Aring;" />
 
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'''PLANT ENZYME CRYSTAL FORM II'''<br />
 
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==Overview==
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==Plant enzyme crystal form II==
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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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<StructureSection load='2c7z' size='340' side='right'caption='[[2c7z]], [[Resolution|resolution]] 2.37&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2c7z]] 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=2C7Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C7Z FirstGlance]. <br>
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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]] 2.37&#8491;</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=2c7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c7z OCA], [https://pdbe.org/2c7z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c7z RCSB], [https://www.ebi.ac.uk/pdbsum/2c7z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c7z ProSAT]</span></td></tr>
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</table>
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== Function ==
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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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== 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/c7/2c7z_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2c7z 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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==About this Structure==
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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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2C7Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C7Z OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16630629 16630629]
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</div>
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[[Category: Acetyl-CoA C-acyltransferase]]
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<div class="pdbe-citations 2c7z" style="background-color:#fffaf0;"></div>
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[[Category: Arabidopsis thaliana]]
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[[Category: Single protein]]
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[[Category: Alphey, M.S.]]
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[[Category: Hunter, W.N.]]
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[[Category: Leonard, G.A.]]
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[[Category: Micossi, E.]]
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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://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:02:23 2007''
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==See Also==
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*[[Thiolase 3D structures|Thiolase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Arabidopsis thaliana]]
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[[Category: Large Structures]]
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[[Category: Alphey MS]]
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[[Category: Hunter WN]]
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[[Category: Leonard GA]]
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[[Category: Micossi E]]
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[[Category: Sundaramoorthy R]]

Current revision

Plant enzyme crystal form II

PDB ID 2c7z

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