6A4X

Oxidase ChaP-H2

6A4X の概要

• エントリーDOI: 10.2210/pdb6a4x/pdb
• 分子名称: Bleomycin resistance protein, FE (II) ION (3 entities in total)
• 機能のキーワード: voc family, dioxygenase, dimer, chartreusin, oxidative rearrangement, biosynthetic protein
• 由来する生物種: Streptomyces curacoi
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14424.68

構造登録者

Zhang, B.,Wang, Y.S.,Ge, H.M. (登録日: 2018-06-21, 公開日: 2018-08-29, 最終更新日: 2023-11-22)

主引用文献

Wang, Y.S.,Zhang, B.,Zhu, J.,Yang, C.L.,Guo, Y.,Liu, C.L.,Liu, F.,Huang, H.,Zhao, S.,Liang, Y.,Jiao, R.H.,Tan, R.X.,Ge, H.M.
Molecular Basis for the Final Oxidative Rearrangement Steps in Chartreusin Biosynthesis.
J. Am. Chem. Soc., 140:10909-10914, 2018

PubMed Abstract: Oxidative rearrangements play key roles in introducing structural complexity and biological activities of natural products biosynthesized by type II polyketide synthases (PKSs). Chartreusin (1) is a potent antitumor polyketide that contains a unique rearranged pentacyclic aromatic bilactone aglycone derived from a type II PKS. Herein, we report an unprecedented dioxygenase, ChaP, that catalyzes the final α-pyrone ring formation in 1 biosynthesis using flavin-activated oxygen as an oxidant. The X-ray crystal structures of ChaP and two homologues, docking studies, and site-directed mutagenesis provided insights into the molecular basis of the oxidative rearrangement that involves two successive C-C bond cleavage steps followed by lactonization. ChaP is the first example of a dioxygenase that requires a flavin-activated oxygen as a substrate despite lacking flavin binding sites, and represents a new class in the vicinal oxygen chelate enzyme superfamily.

PubMed: 30067334
DOI: 10.1021/jacs.8b06623

実験手法

X-RAY DIFFRACTION (1.63 Å)