View source for 1icq

[[Image:1icq.jpg|left|200px]]<br /><applet load="1icq" size="450" color="white" frame="true" align="right" spinBox="true" 
caption="1icq, resolution 2.0&Aring;" />
'''CRYSTAL STRUCTURE OF 12-OXOPHYTODIENOATE REDUCTASE 1 FROM TOMATO COMPLEXED WITH 9R,13R-OPDA'''<br />

==Overview==
BACKGROUND: 12-Oxophytodienoate reductase (OPR) is a flavin mononucleotide, (FMN)-dependent oxidoreductase in plants that belongs to the family of Old, Yellow Enzyme (OYE). It was initially characterized as an enzyme involved, in the biosynthesis of the plant hormone jasmonic acid, where it catalyzes, the reduction of the cyclic fatty acid derivative, 9S,13S-12-oxophytodienoate (9S,13S-OPDA) to, 1S,2S-3-oxo-2(2'[Z]-pentenyl)-cyclopentane-1-octanoate. Several isozymes, of OPR are now known that show different stereoselectivities with regard, to the four stereoisomers of OPDA. RESULTS: Here, we report the, high-resolution crystal structure of OPR1 from Lycopersicon esculentum and, its complex structures with the substrate 9R,13R-OPDA and with, polyethylene glycol 400. OPR1 crystallizes as a monomer and folds into a, (betaalpha)(8) barrel with an overall structure similar to OYE. The, cyclopentenone ring of 9R,13R-OPDA is stacked above the flavin and, activated by two hydrogen bonds to His187 and His190. The olefinic bond is, properly positioned for hydride transfer from the FMN N(5) and proton, transfer from Tyr192 to Cbeta and Calpha, respectively. Comparison of the, OPR1 and OYE structures reveals striking differences in the loops, responsible for binding 9R,13R-OPDA in OPR1. CONCLUSIONS: Despite, extensive biochemical characterization, the physiological function of OYE, still remains unknown. The similar catalytic cavity structures and the, substrate binding mode in OPR1 strongly support the assumption that, alpha,beta-unsaturated carbonyl compounds are physiological substrates of, the OYE family. The specific binding of 9R,13R-OPDA by OPR1 explains the, experimentally observed stereoselectivity and argues in favor of, 9R,13R-OPDA or a structurally related oxylipin as natural substrate of, OPR1.

==About this Structure==
1ICQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Solanum_lycopersicum Solanum lycopersicum] with FMN and OPD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/12-oxophytodienoate_reductase 12-oxophytodienoate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.42 1.3.1.42] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ICQ OCA]. 

==Reference==
X-ray structure of 12-oxophytodienoate reductase 1 provides structural insight into substrate binding and specificity within the family of OYE., Breithaupt C, Strassner J, Breitinger U, Huber R, Macheroux P, Schaller A, Clausen T, Structure. 2001 May 9;9(5):419-29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11377202 11377202]
[[Category: 12-oxophytodienoate reductase]]
[[Category: Single protein]]
[[Category: Solanum lycopersicum]]
[[Category: Breithaupt, C.]]
[[Category: Breitinger, U.]]
[[Category: Clausen, T.]]
[[Category: Huber, R.]]
[[Category: Macheroux, P.]]
[[Category: Schaller, A.]]
[[Category: Strassner, J.]]
[[Category: FMN]]
[[Category: OPD]]
[[Category: 13r-opda)-complex]]
[[Category: beta-alpha-barrel]]
[[Category: fmn-substrate-complex]]
[[Category: protein-fmn-(9r]]

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