期刊
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
卷 77, 期 -, 页码 921-932出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2059798321005040
关键词
Rieske nonheme iron oxygenase; NAD(P)H:ferredoxin oxidoreductase; ferredoxin; Janthinobacterium sp. J3; carbazole 1,9a-dioxygenase; CARDO; electron transfer
资金
- Ministry of Education, Culture, Sports, Science and Technology of Japan [17380052, 20248010]
- Institute for Bioinformatics Research Development, Japan Science Technology Agency (BIRD-JST)
- Grants-in-Aid for Scientific Research [17380052, 20248010] Funding Source: KAKEN
The study resolved two crystal structures of class III CARDO-R, revealing the absence of FAD in the type II structure and significant conformational changes to the FAD-binding domain and C-terminus. Docking simulation of NADH into CARDO-R-J3 suggested that shifts of residues at the C-terminus may facilitate electron transfer. Differences in domain arrangement compared to RO reductases from the ferredoxin-NADP reductase family may correspond to differences in structures of redox partners.
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-J3). 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-J3 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.
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