7C3B

Ferredoxin reductase in carbazole 1,9a-dioxygenase (FAD apo form)

Summary for 7C3B

• Entry DOI: 10.2210/pdb7c3b/pdb
• Descriptor: Ferredoxin reductase component of carbazole, FE2/S2 (INORGANIC) CLUSTER, IODIDE ION, ... (7 entities in total)
• Functional Keywords: rieske non-heme iron oxygenase; nad(p)h:ferredoxin oxidoreductase; ferredoxin; electron transfer; carbazole, oxidoreductase
• Biological source: Janthinobacterium sp. (strain J3)
• Total number of polymer chains: 3
• Total formula weight: 112314.06

Authors

Ashikawa, Y.,Fujimoto, Z.,Nojiri, H. (deposition date: 2020-05-11, release date: 2021-05-26, Last modification date: 2024-05-29)

Primary citation

Ashikawa, Y.,Fujimoto, Z.,Inoue, K.,Yamane, H.,Nojiri, H.
Crystal structure of the ferredoxin reductase component of carbazole 1,9a-dioxygenase from Janthinobacterium sp. J3.
Acta Crystallogr D Struct Biol, 77:921-932, 2021

PubMed Abstract: Carbazole 1,9a-dioxygenase (CARDO), which consists of an oxygenase component and the electron-transport components ferredoxin (CARDO-F) and ferredoxin reductase (CARDO-R), is a Rieske nonheme iron oxygenase (RO). ROs are classified into five subclasses (IA, IB, IIA, IIB and III) based on their number of constituents and the nature of their redox centres. In this study, two types of crystal structure (type I and type II) were resolved of the class III CARDO-R from Janthinobacterium sp. J3 (CARDO-R). Superimposition of the type I and type II structures revealed the absence of flavin adenine dinucleotide (FAD) in the type II structure along with significant conformational changes to the FAD-binding domain and the C-terminus, including movements to fill the space in which FAD had been located. Docking simulation of NADH into the FAD-bound form of CARDO-R suggested that shifts of the residues at the C-terminus caused the nicotinamide moiety to approach the N5 atom of FAD, which might facilitate electron transfer between the redox centres. Differences in domain arrangement were found compared with RO reductases from the ferredoxin-NADP reductase family, suggesting that these differences correspond to differences in the structures of their redox partners ferredoxin and terminal oxygenase. The results of docking simulations with the redox partner class III CARDO-F from Pseudomonas resinovorans CA10 suggested that complex formation suitable for efficient electron transfer is stabilized by electrostatic attraction and complementary shapes of the interacting regions.

PubMed: 34196618
DOI: 10.1107/S2059798321005040

Experimental method

X-RAY DIFFRACTION (2.4 Å)