2ix5: Difference between revisions
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< | ==Short chain specific acyl-CoA oxidase from Arabidopsis thaliana, ACX4 in complex with acetoacetyl-CoA== | ||
<StructureSection load='2ix5' size='340' side='right'caption='[[2ix5]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
You may | == Structural highlights == | ||
<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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> | |||
<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> | |||
<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> | |||
</table> | |||
== Function == | |||
[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). | |||
== 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/ix/2ix5_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=2ix5 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2ix5" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
== | |||
< | |||
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: Arent | [[Category: Large Structures]] | ||
[[Category: Henriksen | [[Category: Arent S]] | ||
[[Category: Mackenzie | [[Category: Henriksen A]] | ||
[[Category: Pedersen | [[Category: Mackenzie J]] | ||
[[Category: Pedersen L]] | |||
Latest revision as of 17:28, 13 December 2023
Short chain specific acyl-CoA oxidase from Arabidopsis thaliana, ACX4 in complex with acetoacetyl-CoAShort chain specific acyl-CoA oxidase from Arabidopsis thaliana, ACX4 in complex with acetoacetyl-CoA
Structural highlights
FunctionACOX4_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). 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 PubMedPlants 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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