2de6
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The reduced complex between oxygenase and ferredoxin in carbazole 1,9a-dioxygenase
OverviewOverview
Carbazole 1,9a-dioxygenase (CARDO), a member of the Rieske nonheme iron, oxygenase system (ROS), consists of a terminal oxygenase (CARDO-O) and, electron transfer components (ferredoxin [CARDO-F] and ferredoxin, reductase [CARDO-R]). We determined the crystal structures of the, nonreduced, reduced, and substrate-bound binary complexes of CARDO-O with, its electron donor, CARDO-F, at 1.9, 1.8, and 2.0 A resolutions, respectively. These structures provide the first structure-based, interpretation of intercomponent electron transfer between two Rieske, [2Fe-2S] clusters of ferredoxin and oxygenase in ROS. Three molecules of, CARDO-F bind to the subunit boundary of one CARDO-O trimeric molecule, and, specific binding created by electrostatic and hydrophobic interactions, with conformational changes suitably aligns the two Rieske clusters for, electron transfer. Additionally, conformational changes upon binding, carbazole resulted in the closure of a lid over the substrate-binding, pocket, thereby seemingly trapping carbazole at the substrate-binding, site.
About this StructureAbout this Structure
2DE6 is a Protein complex structure of sequences from Janthinobacterium and Pseudomonas resinovorans with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Electron transfer complex formation between oxygenase and ferredoxin components in Rieske nonheme iron oxygenase system., Ashikawa Y, Fujimoto Z, Noguchi H, Habe H, Omori T, Yamane H, Nojiri H, Structure. 2006 Dec;14(12):1779-89. PMID:17161368
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