4NAO

Crystal structure of EasH

4NAO の概要

• エントリーDOI: 10.2210/pdb4nao/pdb
• 関連するPDBエントリー: 2A1X 2OPW
• 分子名称: Putative oxygenase, HEXAETHYLENE GLYCOL, 2-OXOGLUTARIC ACID, ... (6 entities in total)
• 機能のキーワード: jelly-roll fold, fe binding, oxidoreductase
• 由来する生物種: Claviceps purpurea (Ergot fungus)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37396.00

構造登録者

Janke, R.,Havemann, J.,Vogel, D.,Keller, U.,Loll, B. (登録日: 2013-10-22, 公開日: 2014-01-15, 最終更新日: 2024-02-28)

主引用文献

Havemann, J.,Vogel, D.,Loll, B.,Keller, U.
Cyclolization of d-lysergic Acid alkaloid peptides.
Chem.Biol., 21:146-155, 2014

PubMed Abstract: The tripeptide chains of the ergopeptines, a class of pharmacologically important D-lysergic acid alkaloid peptides, are arranged in a unique bicyclic cyclol based on an amino-terminal α-hydroxyamino acid and a terminal orthostructure. D-lysergyl-tripeptides are assembled by the nonribosomal peptide synthetases LPS1 and LPS2 of the ergot fungus Claviceps purpurea and released as N-(D-lysergyl-aminoacyl)-lactams. We show total enzymatic synthesis of ergopeptines catalyzed by a Fe²⁺/2-ketoglutarate-dependent dioxygenase (EasH) in conjunction with LPS1/LPS2. Analysis of the reaction indicated that EasH introduces a hydroxyl group into N-(D-lysergyl-aminoacyl)-lactam at α-C of the aminoacyl residue followed by spontaneous condensation with the terminal lactam carbonyl group. Sequence analysis revealed that EasH belongs to the wide and diverse family of the phytanoyl coenzyme A hydroxylases. We provide a high-resolution crystal structure of EasH that is most similar to that of phytanoyl coenzyme A hydroxylase, PhyH, from human.

PubMed: 24361048
DOI: 10.1016/j.chembiol.2013.11.008

実験手法

X-RAY DIFFRACTION (1.649 Å)