2ix5: Difference between revisions

Revision as of 03:00, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ix5.png

Template:STRUCTURE 2ix5

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

Template:ABSTRACT PUBMED 16887802

About this StructureAbout this Structure

2IX5 is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Mon Jul 28 02:59:52 2008

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OCA

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-[[Image:2ix5.gif|left|200px]]
+{{Seed}}
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 {{STRUCTURE_2ix5|  PDB=2ix5  |  SCENE=  }}
-'''SHORT CHAIN SPECIFIC ACYL-COA OXIDASE FROM ARABIDOPSIS THALIANA, ACX4 IN COMPLEX WITH ACETOACETYL-COA'''
+===SHORT CHAIN SPECIFIC ACYL-COA OXIDASE FROM ARABIDOPSIS THALIANA, ACX4 IN COMPLEX WITH ACETOACETYL-COA===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16887802}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16887802 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16887802}}
 ==About this Structure==
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 [[Category: Oxidoreductase]]
 [[Category: Peroxisome]]
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