7VWT
Carbazole Prenyl Transferase CqsB4
7VWT の概要
| エントリーDOI | 10.2210/pdb7vwt/pdb |
| 分子名称 | CqsB4, GLYCEROL, DI(HYDROXYETHYL)ETHER, ... (6 entities in total) |
| 機能のキーワード | prenyl transferase, squalene synthase, transferase |
| 由来する生物種 | Streptomyces sp. |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 78064.03 |
| 構造登録者 | Suemune, H.,Nagata, R.,Kuzuyama, T.,Nagano, S. (登録日: 2021-11-11, 公開日: 2022-03-23, 最終更新日: 2024-04-03) |
| 主引用文献 | Nagata, R.,Suemune, H.,Kobayashi, M.,Shinada, T.,Shin-Ya, K.,Nishiyama, M.,Hino, T.,Sato, Y.,Kuzuyama, T.,Nagano, S. Structural Basis for the Prenylation Reaction of Carbazole-Containing Natural Products Catalyzed by Squalene Synthase-Like Enzymes. Angew.Chem.Int.Ed.Engl., 61:e202117430-e202117430, 2022 Cited by PubMed Abstract: Some enzymes annotated as squalene synthase catalyze the prenylation of carbazole-3,4-quinone-containing substrates in bacterial secondary metabolism. Their reaction mechanisms remain unclear because of their low sequence similarity to well-characterized aromatic substrate prenyltransferases (PTs). We determined the crystal structures of the carbazole PTs, and these revealed that the overall structure is well superposed on those of squalene synthases. In contrast, the stacking interaction between the prenyl donor and acceptor substrates resembles those observed in aromatic substrate PTs. Structural and mutational analyses suggest that the Ile and Asp residues are essential for the hydrophobic and hydrophilic interactions with the carbazole-3,4-quinone moiety of the prenyl acceptor, respectively, and a deprotonation mechanism of an intermediary σ-complex involving a catalytic triad is proposed. Our results provide a structural basis for a new subclass of aromatic substrate PTs. PubMed: 35235232DOI: 10.1002/anie.202117430 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.73 Å) |
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