X‐ray structure of <i>Arabidopsis</i> At1g77680, 12‐oxophytodienoate reductase isoform 1

Fox, Brian G.; Malone, Thomas E.; Johnson, Kenneth A.; Madson, Stacey E.; Aceti, David J.; Bingman, C.A.; Blommel, Paul G.; Buchan, Blake W.; Burns, Brendan T.; Cao, John Z.; Cornilescu, Claudia C.; Doreleijers, Jurgen F.; Ellefson, Jason; Frederick, Ronnie O.; Geetha, H.M; Hruby, David; Jeon, Won Bae; Kimball, Todd; Kunert, John; Markley, John L.; Newman, Christopher; Olson, Andrew; Peterson, Francis C.; Phillips, George N.; Primm, John G.; Ramirez, Bryan; Rosenberg, Nathan; Runnels, Mike; Seder, Kory D.; Shaw, J. Grace; Smith, David W.; Sreenath, Hassan K.; Song, Jikui; Sussman, Michael R.; Thao, Sandy; Troestler, Donna; Tyler, Ejan M.; Tyler, Robert C.; Ulrich, Eldon L.; Vinarov, Dimitriy; Vojtik, Frank C.; Volkman, Brian F.; Wesenberg, G.E.; Wrobel, Russell L.; Zhang, Jie; Zhao, Qin; Zolnai, Zolt

doi:10.1002/prot.20533

Cited by 9 publications

(11 citation statements)

References 16 publications

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“…3b). This structural correspondence is also found for nearly all structurally characterized members of the OYE family (data not shown) with the exception of His-188, which is replaced by asparagine in several enzymes (19,20,(25)(26)(27)(28). The corresponding atoms Asn N␦2 and His N␦1 that bind the carbonyl oxygen overlay perfectly, however, indicating a similar effect on substrate activation and positioning.…”

Section: Resultssupporting

confidence: 66%

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

Breithaupt

Kurzbauer

Lilie

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

114

109

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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.flavoprotein ͉ jasmonic acid biosynthesis ͉ plant defense ͉ oxylipin signature ͉ 12-oxophytodienoic acid F lavoproteins catalyze a wide variety of essential biochemical reactions, including electron transfer, dehydrogenation, and hydroxylation reactions. Old yellow enzyme (OYE), the first flavin-dependent enzyme identified (1), and homologues of OYE from bacteria, yeast, and plants are able to reduce the CAC double bond of ␣,␤-unsaturated carbonyl compounds, an activity that is rather uncommon for flavoenzymes (2, 3). This reaction has been shown to proceed by a ping-pong bi-bi mechanism, during which the FMN cofactor is reduced by NAD(P)H before the substrate is bound and reduced by hydride transfer to the substrate's C ␤ (4). Despite extensive efforts, the physiological substrate has been revealed only for one member of the OYE family, the plant enzyme 12-oxophytodienoate reductase (OPR) 3, which catalyzes one step in the biosynthesis of the plant hormone jasmonic acid (JA) (5, 6). JA and JA derivatives act as signaling compounds in the defense response against herbivores and pathogens and are involved in the regulation of various developmental processes, such as fruit ripening, pollen maturation, and senescence (7,8). JA is synthesized from ␣-linolenic acid, which is oxidized and cyclized, resulting in the cyclopentenone 9S,13S-12-oxophytodienoate (9S,13S-OPDA). OPR3 reduces 9S,13S-OPDA to the corresponding cyclopentanone, which is converted to JA by repeated ␤-oxidation ( Fig. 1) (9). Several OPR isozymes have been identified in plants, including 3 isoforms in Lycopersicon esculentum, 5 in Arabidopsis thaliana, and 13 in Oryza sativa (10, 11). O...

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Section: Resultssupporting

confidence: 66%

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

Breithaupt

Kurzbauer

Lilie

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

114

109

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show abstract

“…The analysis of crystal structures of tomato OPR1 and OPR3 provided insights into the mechanism of substrate reduction and the remarkable differences in stereoselectivity with respect to OPDA isomers (Breithaupt et al, 2001(Breithaupt et al, , 2006Fox et al, 2005;Malone et al, 2005). Consistent with the reaction mechanism proposed for the related Old Yellow Enzyme from yeast, the carbonyl moiety of the substrate forms hydrogen bonds with two histidine residues (His186 and His189 in Arabidopsis OPR1) which leads to a polarization of the a,b-double bond.…”

Section: -Oxophytodienoate Reductase 3 (Opr3)mentioning

confidence: 57%

Enzymes in jasmonate biosynthesis – Structure, function, regulation

2009

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“…(A) Posterior probabilities for site classes with positive-selection pressures (measured by the ω ratio) for amino acid sites along the sequence. The OPR sequence of the Oxidored_FMN domain is shown below the x-axis along with its secondary structure elements corresponding to the structure of AtOPR1/3 [ 64 , 65 ] and LeOPR3 [ 66 ]. Eight α / β -barrel domains are represented as colored tubes and arrows, respectively, and each α / β -barrel is defined as one super secondary structure unit (SSSU).…”

Section: Resultsmentioning

confidence: 99%

Phylogenetic analysis, structural evolution and functional divergence of the 12-oxo-phytodienoate acid reductase gene family in plants

Liu

et al. 2009

BMC Evol Biol

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X‐ray structure of Arabidopsis At1g77680, 12‐oxophytodienoate reductase isoform 1

Cited by 9 publications

References 16 publications

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

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

Enzymes in jasmonate biosynthesis – Structure, function, regulation

Phylogenetic analysis, structural evolution and functional divergence of the 12-oxo-phytodienoate acid reductase gene family in plants

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