5DAV: Fe(ii)/(alpha)ketoglutarate-dependent Dioxygenase Asqj In Complex With 4-methoxydehydrocyclopeptin

Citation:
Abstract
Multienzymatic cascades are responsible for the biosynthesis of natural products and represent a source of inspiration for synthetic chemists. The Fe(II) /alpha-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.
PDB ID: 5DAVDownload
MMDB ID: 134438
PDB Deposition Date: 2015/8/20
Updated in MMDB: 2015/11
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 5DAV: dimeric; determined by author and by software (PISA)
Molecular Components in 5DAV
Label Count Molecule
Proteins (2 molecules)
2
Phytanoyl-coa Dioxygenase Family Protein (Afu_orthologue Afua_8g00230)(Gene symbol: AN9227.2)
Molecule annotation
Chemicals (12 molecules)
1
2
2
2
3
2
4
4
5
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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