2ix5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2ix5.gif|left|200px]]<br /><applet load="2ix5" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2ix5.gif|left|200px]]
-
caption="2ix5, resolution 2.70&Aring;" />
+
 
-
'''SHORT CHAIN SPECIFIC ACYL-COA OXIDASE FROM ARABIDOPSIS THALIANA, ACX4 IN COMPLEX WITH ACETOACETYL-COA'''<br />
+
{{Structure
 +
|PDB= 2ix5 |SIZE=350|CAPTION= <scene name='initialview01'>2ix5</scene>, resolution 2.70&Aring;
 +
|SITE= <scene name='pdbsite=AC1:Fad+Binding+Site+For+Chain+D'>AC1</scene>
 +
|LIGAND= <scene name='pdbligand=CAA:ACETOACETYL-COENZYME+A'>CAA</scene> and <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene>
 +
|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]
 +
|GENE=
 +
}}
 +
 
 +
'''SHORT CHAIN SPECIFIC ACYL-COA OXIDASE FROM ARABIDOPSIS THALIANA, ACX4 IN COMPLEX WITH ACETOACETYL-COA'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
2IX5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with <scene name='pdbligand=CAA:'>CAA</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AC1:Fad+Binding+Site+For+Chain+D'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IX5 OCA].
+
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].
==Reference==
==Reference==
-
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16887802 16887802]
+
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]
[[Category: Acyl-CoA oxidase]]
[[Category: Acyl-CoA oxidase]]
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
Line 33: Line 42:
[[Category: peroxisome]]
[[Category: peroxisome]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:56:56 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:34:30 2008''

Revision as of 15:34, 20 March 2008


PDB ID 2ix5

Drag the structure with the mouse to rotate
, resolution 2.70Å
Sites:
Ligands: and
Activity: Acyl-CoA oxidase, with EC number 1.3.3.6
Coordinates: save as pdb, mmCIF, xml



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.

About this Structure

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

Reference

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 Thu Mar 20 17:34:30 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools