5Z4E
An anthrahydroquino-Gama-pyrone synthase Txn09
5Z4E の概要
| エントリーDOI | 10.2210/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 | |
| 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: 30151879DOI: 10.1002/anie.201806729 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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