PDBsum entry 1w07

Oxidoreductase

PDB id: 1w07

Contents

Protein chains

655 a.a. *

Ligands

FAD ×2

Metals

_PT ×6

_CA

_CL ×2

Waters ×748

* Residue conservation analysis

PDB id:

1w07

Name:

Oxidoreductase

Title:

Arabidopsis thaliana acyl-coa oxidase 1

Structure:

Acyl-coa oxidase. Chain: a, b. Engineered: yes. Mutation: yes

Source:

Arabidopsis thaliana. Mouse-ear cress. Organism_taxid: 3702. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Biol. unit:

Dimer (from PDB file)

Resolution:

2.00Å R-factor: 0.204 R-free: 0.249

Authors:

A.Henriksen,L.Pedersen

Key ref:

L.Pedersen and A.Henriksen (2005). Acyl-CoA oxidase 1 from Arabidopsis thaliana. Structure of a key enzyme in plant lipid metabolism. J Mol Biol, 345, 487-500. PubMed id: 15581893 DOI: 10.1016/j.jmb.2004.10.062

Date:

01-Jun-04 Release date: 15-Dec-04

Protein chains

O65202  (ACOX1_ARATH) -  Peroxisomal acyl-coenzyme A oxidase 1 from Arabidopsis thaliana

Seq: 664 a.a.

Struc: 655 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.1.3.3.6 - acyl-CoA oxidase.
• Reaction: a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2
• Cofactor: FAD

FAD (Bound ligand (Het Group name = FAD) corresponds exactly)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.jmb.2004.10.062

J Mol Biol 345:487-500 (2005)

PubMed id: 15581893

Acyl-CoA oxidase 1 from Arabidopsis thaliana. Structure of a key enzyme in plant lipid metabolism.

L.Pedersen, A.Henriksen.

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.

Selected figure(s)

Figure 5.
Figure 5. Fatty acid-binding pockets of ACX1 and MCAD. a, Surface-accessible area of the fatty acyl-CoA binding pocket in ACX1. The C8-CoA molecule shown in gray originates from a superposition with the MCAD:C8- CoA complex. The flavin ring of the FAD molecule is seen in the lower right corner of the pocket. b, Surface- accessible area of the corresponding pocket in the MCAD:C8-CoA complex. The program msms 56 was used to generate the solvent-accessible surfaces and the Figure was prepared with the program DINO (http:// www.bioz.unibas.ch/~xray/dino).

Figure 6.
Figure 6. ACX1 anion site. The site is located at the dimer interface and involves residues from the N b domain. The residues contributing to the site are conserved within a sub-group of ACXs. Dotted black lines indicate hydrogen bonds and anion interactions. Water molecules are included as gray spheres.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2005, 345, 487-500) copyright 2005.

Figures were selected by an automated process.