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2DE6

The reduced complex between oxygenase and ferredoxin in carbazole 1,9a-dioxygenase

Summary for 2DE6
Entry DOI10.2210/pdb2de6/pdb
Related2DE5 2DE7
Descriptorterminal oxygenase component of carbazole, ferredoxin component of carbazole, FE (II) ION, ... (5 entities in total)
Functional Keywordselectron transfer complex, rieske non-heme iron oxygenase system, terminal oxygenase, rieske-type ferredoxin, carbazole 1, 9a-dioxygenase, oxidoreductase
Biological sourceJanthinobacterium
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Total number of polymer chains6
Total formula weight173298.85
Authors
Ashikawa, Y.,Nojiri, H. (deposition date: 2006-02-08, release date: 2006-12-05, Last modification date: 2023-10-25)
Primary citationAshikawa, 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: 17161368
DOI: 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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