Crystal structure of 12-oxophytodienoate reductase 3 from tomato: Self-inhibition by dimerization

被引:100
作者
Breithaupt, Constanze [1 ]
Kurzbauer, Robert
Lilie, Hauke
Schaller, Andreas
Strassner, Jochen
Huber, Robert
Macheroux, Peter
Clausen, Tim
机构
[1] Max Planck Inst Biochem, Abt Strukturforsch, D-52152 Martinsried, Germany
[2] Res Inst Mol Pathol, A-1030 Vienna, Austria
[3] Univ Halle Wittenberg, Inst Biotechnol, D-06120 Halle, Saale, Germany
[4] Univ Hohenheim, Inst Plant Physiol & Biotechnol 260, D-70593 Stuttgart, Germany
[5] Altana Pharma AG, D-78467 Constance, Germany
[6] Graz Univ, Inst Biochem, A-8010 Graz, Austria
关键词
flavoprotein; jasmonic acid biosynthesis; plant defense; oxylipin signature; 12-oxophytodienoic acid;
D O I
10.1073/pnas.0606603103
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
12-Oxophytodienoate reductase (OPR) 3, a homologue of old yellow enzyme (OYE), catalyzes the reduction of 9S,13S-12-oxophytodienoate to the corresponding cyclopentanone, which is subsequently converted to the plant hormone jasmonic acid (JA). JA and JA derivatives, as well as 12-oxophytodienoate and related cyclopentenones, are known to regulate gene expression in plant development and defense. Together with other oxygenated fatty acid derivatives, they form the oxylipin signature in plants, which resembles the pool of prostaglandins in animals. Here, we report the crystal structure of OPR3 from tomato and of two OPR3 mutants. Although the catalytic residues of OPR3 and related OYEs are highly conserved, several characteristic differences can be discerned in the substrate-binding regions, explaining the remarkable substrate stereoselectivity of OPR isozymes. Interestingly, OPR3 crystallized as an extraordinary self-inhibited dimer. Mutagenesis studies and biochemical analysis confirmed a weak dimerization of OPR3 in vitro, which correlated with a loss of enzymatic activity. Based on structural data of OPR3, a putative mechanism for a strong and reversible dimerization of OPR3 in vivo that involves phosphorylation of OPR3 is suggested. This mechanism could contribute to the shaping of the oxylipin signature, which is critical for fine-tuning gene expression in plants.
引用
收藏
页码:14337 / 14342
页数:6
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