5DAX

Fe(II)/(alpha)ketoglutarate-dependent dioxygenase AsqJ in complex with demethylated cyclopeptin

Summary for 5DAX

• Entry DOI: 10.2210/pdb5dax/pdb
• Related: 5DAP
• Descriptor: Phytanoyl-CoA dioxygenase family protein (AFU_orthologue AFUA_8G00230), NICKEL (II) ION, 2-OXOGLUTARIC ACID, ... (5 entities in total)
• Functional Keywords: antibiotics, biosynthesis, alkaloids, viridicatin, desaturase, epoxidase, fragmentation, demethylated cyclopeptin, oxidoreductase
• Biological source: Aspergillus nidulans FGSC A4
• Total number of polymer chains: 1
• Total formula weight: 34449.94

Authors

Groll, M.,Braeuer, A. (deposition date: 2015-08-20, release date: 2015-11-25, Last modification date: 2024-01-10)

Primary citation

Brauer, A.,Beck, P.,Hintermann, L.,Groll, M.
Structure of the Dioxygenase AsqJ: Mechanistic Insights into a One-Pot Multistep Quinolone Antibiotic Biosynthesis.
Angew.Chem.Int.Ed.Engl., 55:422-426, 2016

PubMed Abstract: Multienzymatic cascades are responsible for the biosynthesis of natural products and represent a source of inspiration for synthetic chemists. The Fe(II)/α-ketoglutarate-dependent dioxygenase AsqJ from Aspergillus nidulans is outstanding because it stereoselectively catalyzes both a ferryl-induced desaturation reaction and epoxidation on a benzodiazepinedione. Interestingly, the enzymatically formed spiro epoxide spring-loads the 6,7-bicyclic skeleton for non-enzymatic rearrangement into the 6,6-bicyclic scaffold of the quinolone alkaloid 4'-methoxyviridicatin. Herein, we report different crystal structures of the protein in the absence and presence of synthesized substrates, surrogates, and intermediates that mimic the various stages of the reaction cycle of this exceptional dioxygenase.

PubMed: 26553478
DOI: 10.1002/anie.201507835

Experimental method

X-RAY DIFFRACTION (1.7 Å)