6l8i
From Proteopedia
Crystal structure of CYP97A3 mutant S290D/W300L/S304V
Structural highlights
FunctionLUT5_ARATH Heme-containing cytochrome P450 involved in the biosynthesis of xanthophylls. Specific for beta-ring hydroxylation of alpha- and beta-carotene. Has also a low activity toward the epsilon-rings of alpha-carotene. The beta-ring of alpha-carotene is the preferred substrate in planta.[1] [2] [3] Publication Abstract from PubMedTwo cytochrome P450 enzymes, CYP97A3 and CYP97C1, catalyze hydroxylations of the beta- and epsilon-rings of alpha-carotene to produce lutein. Chirality is introduced at the C-3 atom of both rings, and the reactions are both pro-3R-stereospecific. We determined the crystal structures of CYP97A3 in substrate-free and complex forms with a nonnatural substrate and the structure of CYP97C1 in a detergent-bound form. The structures of CYP97A3 in different states show the substrate channel and the structure of CYP97C1 bound with octylthioglucoside confirms the binding site for the carotenoid substrate. Biochemical assays confirm that the ferredoxin-NADP(+) reductase (FNR)-ferredoxin pair is used as the redox partner. Details of the pro-3R stereospecificity are revealed in the retinal-bound CYP97A3 structure. Further analysis indicates that the CYP97B clan bears similarity to the beta-ring-specific CYP97A clan. Overall, our research describes the molecular basis for the last steps of lutein biosynthesis. Structural basis for plant lutein biosynthesis from alpha-carotene.,Niu G, Guo Q, Wang J, Zhao S, He Y, Liu L Proc Natl Acad Sci U S A. 2020 Jun 23;117(25):14150-14157. doi:, 10.1073/pnas.2001806117. Epub 2020 Jun 8. PMID:32513704[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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