2FON
X-ray crystal structure of LeACX1, an acyl-CoA oxidase from Lycopersicon esculentum (tomato)
Summary for 2FON
| Entry DOI | 10.2210/pdb2fon/pdb |
| Descriptor | peroxisomal acyl-CoA oxidase 1A, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total) |
| Functional Keywords | oxidoreductase, peroxisomal beta-oxidation, fad cofactor |
| Biological source | Solanum lycopersicum |
| Total number of polymer chains | 3 |
| Total formula weight | 231992.38 |
| Authors | Garavito, R.M.,Powers, R.A. (deposition date: 2006-01-13, release date: 2006-05-23, Last modification date: 2024-02-14) |
| Primary citation | Powers, R.A.,Rife, C.L.,Schilmiller, A.L.,Howe, G.A.,Garavito, R.M. Structure determination and analysis of acyl-CoA oxidase (ACX1) from tomato. Acta Crystallogr.,Sect.D, 62:683-686, 2006 Cited by PubMed 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. PubMed: 16699197DOI: 10.1107/S0907444906014107 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.74 Å) |
Structure validation
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