2DE6
The reduced complex between oxygenase and ferredoxin in carbazole 1,9a-dioxygenase
Summary for 2DE6
Entry DOI | 10.2210/pdb2de6/pdb |
Related | 2DE5 2DE7 |
Descriptor | terminal oxygenase component of carbazole, ferredoxin component of carbazole, FE (II) ION, ... (5 entities in total) |
Functional Keywords | electron transfer complex, rieske non-heme iron oxygenase system, terminal oxygenase, rieske-type ferredoxin, carbazole 1, 9a-dioxygenase, oxidoreductase |
Biological source | Janthinobacterium More |
Total number of polymer chains | 6 |
Total formula weight | 173298.85 |
Authors | Ashikawa, Y.,Nojiri, H. (deposition date: 2006-02-08, release date: 2006-12-05, Last modification date: 2023-10-25) |
Primary citation | Ashikawa, Y.,Fujimoto, Z.,Noguchi, H.,Habe, H.,Omori, T.,Yamane, H.,Nojiri, H. Electron Transfer Complex Formation between Oxygenase and Ferredoxin Components in Rieske Nonheme Iron Oxygenase System Structure, 14:1779-1789, 2006 Cited by PubMed Abstract: 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. PubMed: 17161368DOI: 10.1016/j.str.2006.10.004 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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