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7VWT

Carbazole Prenyl Transferase CqsB4

7VWT の概要
エントリーDOI10.2210/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: 35235232
DOI: 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)
構造検証レポート
Validation report summary of 7vwt
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-01-28に公開中

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