Structural insights into 3Fe-4S ferredoxins diversity in M. tuberculosis highlighted by a first redox complex with P450

Ferredoxins are small iron-sulfur proteins and key players in essential metabolic pathways. Among all types, 3Fe-4S ferredoxins are less studied mostly due to anaerobic requirements. Their complexes with cytochrome P450 redox partners have not been structurally characterized. In the present work, we...

Full description

Saved in:
Bibliographic Details
Published in:Frontiers in molecular biosciences 2023-01, Vol.9, p.1100032-1100032
Main Authors: Gilep, Andrei, Varaksa, Tatsiana, Bukhdruker, Sergey, Kavaleuski, Anton, Ryzhykau, Yury, Smolskaya, Sviatlana, Sushko, Tatsiana, Tsumoto, Kouhei, Grabovec, Irina, Kapranov, Ivan, Okhrimenko, Ivan, Marin, Egor, Shevtsov, Mikhail, Mishin, Alexey, Kovalev, Kirill, Kuklin, Alexander, Gordeliy, Valentin, Kaluzhskiy, Leonid, Gnedenko, Oksana, Yablokov, Evgeniy, Ivanov, Alexis, Borshchevskiy, Valentin, Strushkevich, Natallia
Format: Article
Language:English
Subjects:
3Fe–4S ferredoxins
crystal structure
cytochrome P450
Molecular Biosciences
protein–protein interactions
redox complex
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Ferredoxins are small iron-sulfur proteins and key players in essential metabolic pathways. Among all types, 3Fe-4S ferredoxins are less studied mostly due to anaerobic requirements. Their complexes with cytochrome P450 redox partners have not been structurally characterized. In the present work, we solved the structures of both 3Fe-4S ferredoxins from -Fdx alone and the fusion FdxE-CYP143. Our SPR analysis demonstrated a high-affinity binding of FdxE to CYP143. According to SAXS data, the same complex is present in solution. The structure reveals extended multipoint interactions and the shape/charge complementarity of redox partners. Furthermore, FdxE binding induced conformational changes in CYP143 as evident from the solved CYP143 structure alone. The comparison of FdxE-CYP143 and modeled Fdx-CYP51 complexes further revealed the specificity of ferredoxins. Our results illuminate the diversity of electron transfer complexes for the production of different secondary metabolites.
ISSN:2296-889X
2296-889X
DOI:10.3389/fmolb.2022.1100032