1W07

Arabidopsis thaliana acyl-CoA oxidase 1

Summary for 1W07

• Entry DOI: 10.2210/pdb1w07/pdb
• Descriptor: ACYL-COA OXIDASE, FLAVIN-ADENINE DINUCLEOTIDE, CALCIUM ION, ... (6 entities in total)
• Functional Keywords: oxidoreductase, peroxisomal beta-oxidation, fad cofactor
• Biological source: ARABIDOPSIS THALIANA (MOUSE-EAR CRESS)
• Cellular location: Peroxisome : O65202
• Total number of polymer chains: 2
• Total formula weight: 150374.68

Authors

Henriksen, A.,Pedersen, L. (deposition date: 2004-06-01, release date: 2004-12-15, Last modification date: 2024-11-06)

Primary citation

Pedersen, L.,Henriksen, A.
Acyl-Coa Oxidase 1 from Arabidopsis Thaliana. Structure of a Key Enzyme in Plant Lipid Metabolism
J.Mol.Biol., 345:487-, 2005

PubMed Abstract: The peroxisomal acyl-CoA oxidase family plays an essential role in lipid metabolism by catalyzing the conversion of acyl-CoA into trans-2-enoyl-CoA during fatty acid beta-oxidation. Here, we report the X-ray structure of the FAD-containing Arabidopsis thaliana acyl-CoA oxidase 1 (ACX1), the first three-dimensional structure of a plant acyl-CoA oxidase. Like other acyl-CoA oxidases, the enzyme is a dimer and it has a fold resembling that of mammalian acyl-CoA oxidase. A comparative analysis including mammalian acyl-CoA oxidase and the related tetrameric mitochondrial acyl-CoA dehydrogenases reveals a substrate-binding architecture that explains the observed preference for long-chained, mono-unsaturated substrates in ACX1. Two anions are found at the ACX1 dimer interface and for the first time the presence of a disulfide bridge in a peroxisomal protein has been observed. The functional differences between the peroxisomal acyl-CoA oxidases and the mitochondrial acyl-CoA dehydrogenases are attributed to structural differences in the FAD environments.

PubMed: 15581893
DOI: 10.1016/J.JMB.2004.10.062

Experimental method

X-RAY DIFFRACTION (2 Å)