6t2t
Crystal structure of Drosophila melanogaster glutathione S-transferase epsilon 14 in complex with glutathione and 2-methyl-2,4-pentanediol
Structural highlights
FunctionGSTEE_DROME Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles (PubMed:22082028). Essential for ecdysteroid biosynthesis (PubMed:25344753, PubMed:25300303). May be involved in detoxification (PubMed:22082028).[1] [2] [3] Publication Abstract from PubMedEcdysteroids are critically important for the formation of the insect exoskeleton. Cholesterol is a precursor of ecdysone and its active form 20-hydroxyecdysone, but some steps in the ecdysteroid biosynthesis pathway remain unknown. An essential requirement of glutathione (GSH) transferase GSTE14 in ecdysteroid biosynthesis has been established in Drosophila melanogaster, but its function is entirely unknown. Here, we have determined the crystal structure of GSTE14 in complex with GSH and investigated the kinetic properties of GSTE14 with alternative substrates. GSTE14 has high-ranking steroid double-bond isomerase activity, albeit 50-fold lower than the most efficient mammalian GSTs. Corresponding steroid isomerizations are unknown in insects, and their exact physiological role remains to be shown. Nonetheless, the essential enzyme GSTE14 is here demonstrated to be catalytically competent and have a steroid-binding site. Structure and steroid isomerase activity of Drosophila glutathione transferase E14 essential for ecdysteroid biosynthesis.,Skerlova J, Lindstrom H, Gonis E, Sjodin B, Neiers F, Stenmark P, Mannervik B FEBS Lett. 2019 Dec 16. doi: 10.1002/1873-3468.13718. PMID:31845319[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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