2ix6

From Proteopedia

(Difference between revisions)

Current revision

SHORT CHAIN SPECIFIC ACYL-COA OXIDASE FROM ARABIDOPSIS THALIANA, ACX4

Structural highlights

2ix6 is a 6 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.9Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Mackenzie J, Pedersen L, Arent S, Henriksen A. Controlling electron transfer in Acyl-CoA oxidases and dehydrogenases: a structural view. J Biol Chem. 2006 Oct 13;281(41):31012-20. Epub 2006 Aug 3. PMID:16887802 doi:10.1074/jbc.M603405200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ix6"

@@ Line 1: / Line 1: @@
 ==SHORT CHAIN SPECIFIC ACYL-COA OXIDASE FROM ARABIDOPSIS THALIANA, ACX4==
-<StructureSection load='2ix6' size='340' side='right' caption='[[2ix6]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
+<StructureSection load='2ix6' size='340' side='right'caption='[[2ix6]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ix6]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IX6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IX6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ix6]] is a 6 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=2IX6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IX6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.9&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1is2|1is2]], [[1w07|1w07]], [[2ddh|2ddh]], [[2fon|2fon]], [[2ix5|2ix5]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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=2ix6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ix6 OCA], [https://pdbe.org/2ix6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ix6 RCSB], [https://www.ebi.ac.uk/pdbsum/2ix6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ix6 ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ix6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ix6 OCA], [http://pdbe.org/2ix6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ix6 RCSB], [http://www.ebi.ac.uk/pdbsum/2ix6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ix6 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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).
+[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]]
@@ Line 34: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Acyl-CoA oxidase]]
+[[Category: Arabidopsis thaliana]]
-[[Category: Arath]]
+[[Category: Large Structures]]
-[[Category: Arent, S]]
+[[Category: Arent S]]
-[[Category: Henriksen, A]]
+[[Category: Henriksen A]]
-[[Category: Mackenzie, J]]
+[[Category: Mackenzie J]]
-[[Category: Pedersen, L]]
+[[Category: Pedersen L]]
-[[Category: Acx4]]
-[[Category: Acyl-coa oxidase]]
-[[Category: Beta-oxidation]]
-[[Category: Electron transfer]]
-[[Category: Fad]]
-[[Category: Fatty acid metabolism]]
-[[Category: Flavin]]
-[[Category: Flavoprotein]]
-[[Category: Glyoxysome]]
-[[Category: Lipid metabolism]]
-[[Category: Oxidoreductase]]
-[[Category: Peroxisome]]

2ix6

From Proteopedia

Current revision

SHORT CHAIN SPECIFIC ACYL-COA OXIDASE FROM ARABIDOPSIS THALIANA, ACX4

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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