7UQL
Pathogenesis related 10-10 app from
7UQL の概要
エントリーDOI | 10.2210/pdb7uql/pdb |
分子名称 | Pathogenesis Related 10-10 protein (2 entities in total) |
機能のキーワード | binding protein, alkaloids, opium poppy, biosynthetic protein |
由来する生物種 | Papaver somniferum |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 35251.79 |
構造登録者 | |
主引用文献 | Ozber, N.,Carr, S.C.,Morris, J.S.,Liang, S.,Watkins, J.L.,Caldo, K.M.,Hagel, J.M.,Ng, K.K.S.,Facchini, P.J. Alkaloid binding to opium poppy major latex proteins triggers structural modification and functional aggregation. Nat Commun, 13:6768-6768, 2022 Cited by PubMed Abstract: Opium poppy accumulates copious amounts of several benzylisoquinoline alkaloids including morphine, noscapine, and papaverine, in the specialized cytoplasm of laticifers, which compose an internal secretory system associated with phloem throughout the plant. The contiguous latex includes an abundance of related proteins belonging to the pathogenesis-related (PR)10 family known collectively as major latex proteins (MLPs) and representing at least 35% of the total cellular protein content. Two latex MLP/PR10 proteins, thebaine synthase and neopione isomerase, have recently been shown to catalyze late steps in morphine biosynthesis previously assigned as spontaneous reactions. Using a combination of sucrose density-gradient fractionation-coupled proteomics, differential scanning fluorimetry, isothermal titration calorimetry, and X-ray crystallography, we show that the major latex proteins are a family of alkaloid-binding proteins that display altered conformation in the presence of certain ligands. Addition of MLP/PR10 proteins to yeast strains engineered with morphine biosynthetic genes from the plant significantly enhanced the conversion of salutaridine to morphinan alkaloids. PubMed: 36351903DOI: 10.1038/s41467-022-34313-6 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.9 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード
