Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5Z4E

An anthrahydroquino-Gama-pyrone synthase Txn09

5Z4E の概要
エントリーDOI10.2210/pdb5z4e/pdb
NMR情報BMRB: 36154
分子名称TxnO9 (1 entity in total)
機能のキーワードtype ii polyketide heterocyclase, enzyme mechanism, natural product, streptomyces bottropensis, biosynthetic protein
由来する生物種Streptomyces bottropensis
タンパク質・核酸の鎖数1
化学式量合計17451.54
構造登録者
Song, Y.J.,Cao, C.Y. (登録日: 2018-01-11, 公開日: 2018-12-12, 最終更新日: 2024-05-15)
主引用文献Hou, X.F.,Song, Y.J.,Zhang, M.,Lan, W.X.,Meng, S.,Wang, C.X.,Pan, H.X.,Cao, C.Y.,Tang, G.L.
Enzymology of Anthraquinone-gamma-Pyrone Ring Formation in Complex Aromatic Polyketide Biosynthesis.
Angew. Chem. Int. Ed. Engl., 57:13475-13479, 2018
Cited by
PubMed Abstract: Aromatic-fused γ-pyrones are structural features of many bioactive natural products and valid scaffolds for medicinal chemistry. However, the enzymology of their formation has not been completely established. Now it is demonstrated that TxnO9, a CalC-like protein belonging to a START family, functions as an unexpected anthraquinone-γ-pyrone synthase involved in the biosynthesis of antitumor antibiotic trioxacarcin A (TXN-A). Structural analysis by NMR identified a likely substrate/product-binding mode and putative key active sites of TxnO9, which allowed an enzymatic mechanism to be proposed. Moreover, a subset of uncharacterized homologous proteins bearing an unexamined Lys-Thr dyad exhibit the same function. Therefore, the functional assignment and mechanistic investigation of this γ-pyrone synthase elucidated an undescribed step in TXN-A biosynthesis, and the discovery of this new branch of polyketide heterocyclases expands the functions of the START superfamily.
PubMed: 30151879
DOI: 10.1002/anie.201806729
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 5z4e
検証レポート(詳細版)ダウンロードをダウンロード

248335

件を2026-01-28に公開中

PDB statisticsPDBj update infoContact PDBjnumon