2ix5

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[[Image:2ix5.gif|left|200px]]
 
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{{Structure
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==Short chain specific acyl-CoA oxidase from Arabidopsis thaliana, ACX4 in complex with acetoacetyl-CoA==
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|PDB= 2ix5 |SIZE=350|CAPTION= <scene name='initialview01'>2ix5</scene>, resolution 2.70&Aring;
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<StructureSection load='2ix5' size='340' side='right'caption='[[2ix5]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Fad+Binding+Site+For+Chain+D'>AC1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CAA:ACETOACETYL-COENZYME+A'>CAA</scene> and <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene>
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<table><tr><td colspan='2'>[[2ix5]] is a 4 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=2IX5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IX5 FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Acyl-CoA_oxidase Acyl-CoA oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.3.6 1.3.3.6]
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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]] 2.7&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAA:ACETOACETYL-COENZYME+A'>CAA</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
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}}
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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=2ix5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ix5 OCA], [https://pdbe.org/2ix5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ix5 RCSB], [https://www.ebi.ac.uk/pdbsum/2ix5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ix5 ProSAT]</span></td></tr>
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</table>
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'''SHORT CHAIN SPECIFIC ACYL-COA OXIDASE FROM ARABIDOPSIS THALIANA, ACX4 IN COMPLEX WITH ACETOACETYL-COA'''
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== Function ==
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[https://www.uniprot.org/uniprot/ACOX4_ARATH ACOX4_ARATH] Catalyzes the desaturation of short-chain acyl-CoAs to 2-trans-enoyl-CoAs. Active on butyryl-CoA (C4), hexanoyl-CoA (C6), and octanoyl-CoA (C8). Has no activity as acyl-CoA dehydrogenase or on crotonyl-CoA (an unsaturated C4:1 carbocyclic ester) or glutaryl-CoA (a dicarboxylic ester).
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== Evolutionary Conservation ==
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==Overview==
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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/ix/2ix5_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=2ix5 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 ==
Plants produce a unique peroxisomal short chain-specific acyl-CoA oxidase (ACX4) for beta-oxidation of lipids. The short chain-specific oxidase has little resemblance to other peroxisomal acyl-CoA oxidases but has an approximately 30% sequence identity to mitochondrial acyl-CoA dehydrogenases. Two biochemical features have been linked to structural properties by comparing the structures of short chain-specific Arabidopsis thaliana ACX4 with and without a substrate analogue bound in the active site to known acyl-CoA oxidases and dehydrogenase structures: (i) a solvent-accessible acyl binding pocket is not required for oxygen reactivity, and (ii) the oligomeric state plays a role in substrate pocket architecture but is not linked to oxygen reactivity. The structures indicate that the acyl-CoA oxidases may encapsulate the electrons for transfer to molecular oxygen by blocking the dehydrogenase substrate interaction site with structural extensions. A small binding pocket observed adjoining the flavin adenine dinucleotide N5 and C4a atoms could increase the number of productive encounters between flavin adenine dinucleotide and O2.
Plants produce a unique peroxisomal short chain-specific acyl-CoA oxidase (ACX4) for beta-oxidation of lipids. The short chain-specific oxidase has little resemblance to other peroxisomal acyl-CoA oxidases but has an approximately 30% sequence identity to mitochondrial acyl-CoA dehydrogenases. Two biochemical features have been linked to structural properties by comparing the structures of short chain-specific Arabidopsis thaliana ACX4 with and without a substrate analogue bound in the active site to known acyl-CoA oxidases and dehydrogenase structures: (i) a solvent-accessible acyl binding pocket is not required for oxygen reactivity, and (ii) the oligomeric state plays a role in substrate pocket architecture but is not linked to oxygen reactivity. The structures indicate that the acyl-CoA oxidases may encapsulate the electrons for transfer to molecular oxygen by blocking the dehydrogenase substrate interaction site with structural extensions. A small binding pocket observed adjoining the flavin adenine dinucleotide N5 and C4a atoms could increase the number of productive encounters between flavin adenine dinucleotide and O2.
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==About this Structure==
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Controlling electron transfer in Acyl-CoA oxidases and dehydrogenases: a structural view.,Mackenzie J, Pedersen L, Arent S, Henriksen A J Biol Chem. 2006 Oct 13;281(41):31012-20. Epub 2006 Aug 3. PMID:16887802<ref>PMID:16887802</ref>
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2IX5 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=2IX5 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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Controlling electron transfer in Acyl-CoA oxidases and dehydrogenases: a structural view., Mackenzie J, Pedersen L, Arent S, Henriksen A, J Biol Chem. 2006 Oct 13;281(41):31012-20. Epub 2006 Aug 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16887802 16887802]
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</div>
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[[Category: Acyl-CoA oxidase]]
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<div class="pdbe-citations 2ix5" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[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: Arent, S.]]
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[[Category: Arent S]]
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[[Category: Henriksen, A.]]
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[[Category: Henriksen A]]
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[[Category: Mackenzie, J.]]
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[[Category: Mackenzie J]]
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[[Category: Pedersen, L.]]
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[[Category: Pedersen L]]
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[[Category: CAA]]
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[[Category: FAD]]
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[[Category: acx4]]
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[[Category: acyl-coa oxidase]]
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[[Category: beta-oxidation]]
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[[Category: electron transfer]]
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[[Category: fad]]
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[[Category: fatty acid metabolism]]
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[[Category: flavin]]
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[[Category: flavoprotein]]
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[[Category: glyoxysome]]
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[[Category: lipid metabolism]]
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[[Category: oxidoreductase]]
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[[Category: peroxisome]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:34:30 2008''
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Current revision

Short chain specific acyl-CoA oxidase from Arabidopsis thaliana, ACX4 in complex with acetoacetyl-CoA

PDB ID 2ix5

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