2FON

X-ray crystal structure of LeACX1, an acyl-CoA oxidase from Lycopersicon esculentum (tomato)

2FON の概要

• エントリーDOI: 10.2210/pdb2fon/pdb
• 分子名称: peroxisomal acyl-CoA oxidase 1A, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: oxidoreductase, peroxisomal beta-oxidation, fad cofactor
• 由来する生物種: Solanum lycopersicum
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 231992.38

構造登録者

Garavito, R.M.,Powers, R.A. (登録日: 2006-01-13, 公開日: 2006-05-23, 最終更新日: 2024-02-14)

主引用文献

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

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: 16699197
DOI: 10.1107/S0907444906014107

実験手法

X-RAY DIFFRACTION (2.74 Å)