1ICP

CRYSTAL STRUCTURE OF 12-OXOPHYTODIENOATE REDUCTASE 1 FROM TOMATO COMPLEXED WITH PEG400

Summary for 1ICP

• Entry DOI: 10.2210/pdb1icp/pdb
• Related: 1ICQ 1ICS
• Descriptor: 12-OXOPHYTODIENOATE REDUCTASE 1, CHLORIDE ION, SULFATE ION, ... (6 entities in total)
• Functional Keywords: beta-alpha-barrel, protein-fmn-peg complex, oxidoreductase
• Biological source: Solanum lycopersicum
• Cellular location: Cytoplasm: Q9XG54
• Total number of polymer chains: 2
• Total formula weight: 86855.31

Authors

Breithaupt, C.,Strassner, J.,Breitinger, U.,Huber, R.,Macheroux, P.,Schaller, A.,Clausen, T. (deposition date: 2001-04-02, release date: 2001-05-16, Last modification date: 2023-08-09)

Primary citation

Breithaupt, C.,Strassner, J.,Breitinger, U.,Huber, R.,Macheroux, P.,Schaller, A.,Clausen, T.
X-ray structure of 12-oxophytodienoate reductase 1 provides structural insight into substrate binding and specificity within the family of OYE.
Structure, 9:419-429, 2001

PubMed Abstract: 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.

PubMed: 11377202
DOI: 10.1016/S0969-2126(01)00602-5

Experimental method

X-RAY DIFFRACTION (1.9 Å)