2IX5

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

Summary for 2IX5

• Entry DOI: 10.2210/pdb2ix5/pdb
• Related: 1IS2 1W07 2DDH 2FON 2IX6
• Descriptor: ACYL-COENZYME A OXIDASE 4, PEROXISOMAL, ACETOACETYL-COENZYME A, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: fad, acx4, flavin, peroxisome, glyoxysome, fatty acid metabolism, lipid metabolism, acyl-coa oxidase, electron transfer, flavoprotein, beta-oxidation, oxidoreductase
• Biological source: ARABIDOPSIS THALIANA (MOUSE-EAR CRESS)
• Cellular location: Glyoxysome: Q96329
• Total number of polymer chains: 4
• Total formula weight: 196971.58

Authors

Mackenzie, J.,Pedersen, L.,Arent, S.,Henriksen, A. (deposition date: 2006-07-07, release date: 2006-08-08, Last modification date: 2023-12-13)

Primary citation

Mackenzie, J.,Pedersen, L.,Arent, S.,Henriksen, A.
Controlling Electron Transfer in Acyl-Coa Oxidases and Dehydrogenases: A Structural View.
J.Biol.Chem., 281:31012-, 2006

PubMed Abstract: 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.

PubMed: 16887802
DOI: 10.1074/JBC.M603405200

Experimental method

X-RAY DIFFRACTION (2.7 Å)