6A4Z

Oxidase ChaP

Summary for 6A4Z

• Entry DOI: 10.2210/pdb6a4z/pdb
• Descriptor: ChaP protein, FE (II) ION (3 entities in total)
• Functional Keywords: voc family, dioxygenase, dimer, chartreusin, oxidative rearrangement, biosynthetic protein
• Biological source: Streptomyces chartreusis
• Total number of polymer chains: 2
• Total formula weight: 30125.31

Authors

Zhang, B.,Ge, H.M. (deposition date: 2018-06-21, release date: 2018-08-29, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.7 Å)