8AMP
Crystal structure of M.tuberculosis ferredoxin Fdx
8AMP の概要
エントリーDOI | 10.2210/pdb8amp/pdb |
分子名称 | Possible ferredoxin, FE3-S4 CLUSTER, FE (III) ION, ... (4 entities in total) |
機能のキーワード | ferredoxin, electron transport, tuberculosis, rv0763c, cyp51 |
由来する生物種 | Mycobacterium tuberculosis |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 8871.23 |
構造登録者 | Bukhdruker, S.,Kavaleuski, A.,Marin, E.,Kapranov, I.,Mishin, A.,Gilep, A.,Strushkevich, N.,Borshchevskiy, V. (登録日: 2022-08-03, 公開日: 2023-02-15, 最終更新日: 2024-02-07) |
主引用文献 | Gilep, A.,Varaksa, T.,Bukhdruker, S.,Kavaleuski, A.,Ryzhykau, Y.,Smolskaya, S.,Sushko, T.,Tsumoto, K.,Grabovec, I.,Kapranov, I.,Okhrimenko, I.,Marin, E.,Shevtsov, M.,Mishin, A.,Kovalev, K.,Kuklin, A.,Gordeliy, V.,Kaluzhskiy, L.,Gnedenko, O.,Yablokov, E.,Ivanov, A.,Borshchevskiy, V.,Strushkevich, N. Structural insights into 3Fe-4S ferredoxins diversity in M. tuberculosis highlighted by a first redox complex with P450. Front Mol Biosci, 9:1100032-1100032, 2022 Cited by PubMed Abstract: 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. PubMed: 36699703DOI: 10.3389/fmolb.2022.1100032 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2 Å) |
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