6A4X
Oxidase ChaP-H2
Summary for 6A4X
| Entry DOI | 10.2210/pdb6a4x/pdb |
| Descriptor | Bleomycin resistance protein, FE (II) ION (3 entities in total) |
| Functional Keywords | voc family, dioxygenase, dimer, chartreusin, oxidative rearrangement, biosynthetic protein |
| Biological source | Streptomyces curacoi |
| Total number of polymer chains | 1 |
| Total formula weight | 14424.68 |
| Authors | Zhang, B.,Wang, Y.S.,Ge, H.M. (deposition date: 2018-06-21, release date: 2018-08-29, Last modification date: 2023-11-22) |
| 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 Cited by 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: 30067334DOI: 10.1021/jacs.8b06623 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.63 Å) |
Structure validation
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