PDBsum entry: 2fon

Oxidoreductase

PDB id: 2fon

Contents

Protein chains

654 a.a. *

Ligands

FAD ×3

Waters ×36

* Residue conservation analysis

PDB id:

2fon

Name:

Oxidoreductase

Title:

X-ray crystal structure of leacx1, an acyl-coa oxidase from lycopersicon esculentum (tomato)

Structure:

Peroxisomal acyl-coa oxidase 1a. Chain: a, b, c. Engineered: yes

Source:

Solanum lycopersicum. Organism_taxid: 4081. Gene: acx1a. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PDB file)

Resolution:

2.74Å R-factor: 0.212 R-free: 0.267

Authors:

R.M.Garavito,R.A.Powers

Key ref:

R.A.Powers et al. (2006). Structure determination and analysis of acyl-CoA oxidase (ACX1) from tomato. Acta Crystallogr D Biol Crystallogr, 62, 683-686. PubMed id: 16699197 DOI: 10.1107/S0907444906014107

Date:

13-Jan-06 Release date: 23-May-06

Protein chains

Q5D8D3  (Q5D8D3_SOLLC) -  Acyl-coenzyme A oxidase

Seq: 664 a.a.

Struc: 654 a.a.

 Gene Ontology (GO) functional annotation 

• Cellular component: peroxisome (1 term)
• Biological process: metabolic process (4 terms)
• Biochemical function: nucleotide binding (5 terms)

DOI no: 10.1107/S0907444906014107

Acta Crystallogr D Biol Crystallogr 62:683-686 (2006)

PubMed id: 16699197

Structure determination and analysis of acyl-CoA oxidase (ACX1) from tomato.

R.A.Powers, C.L.Rife, A.L.Schilmiller, G.A.Howe, R.M.Garavito.

ABSTRACT

The flavoenzyme acyl-CoA oxidase (ACX) catalyzes the first committed step in beta-oxidation and is required for the biosynthesis of jasmonic acid, a signaling molecule involved in plant defense. Recently, a mutant in tomato was identified that is deficient in jasmonic acid production and compromised in its wound response. This results from a single point mutation in acx1, which causes the conserved residue Thr138 to be substituted by isoleucine. To understand the structural basis for this mutation, the crystal structure of LeACX1 was determined to 2.74 Angstrom resolution by molecular replacement. Unexpectedly, an unusual packing arrangement was observed in which three monomers of LeACX1 are present in the asymmetric unit. Although the tertiary structure of LeACX1 is essentially similar to the previously determined structures of ACX enzymes, the packing within the unit cells is distinctly different.

Selected figure(s)

Figure 1.
Figure 1 Representation of the unusual packing arrangement of LeACX1 with three monomers, essentially one full and one half of the biological dimer, in the asymmetric unit. The third monomer in the asymmetric unit (C) forms a dimer across a crystallographic twofold (denoted by a black oval), thereby generating the homodimeric biological molecule. All figures were created with PyMOL (DeLano, 2002[DeLano, W. L. (2002). The PyMOL Molecular Graphics System, v.0.98. http://www.pymol.org .]).

The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2006, 62, 683-686) copyright 2006.

Figure was selected by the author.