Back to Search
Start Over
The oxygenating constituent of 3,6-diketocamphane monooxygenase from the CAM plasmid ofPseudomonas putida: the first crystal structure of a type II Baeyer–Villiger monooxygenase. Corrigendum
- Source :
- Acta Crystallographica Section D: Biological Crystallography
- Publication Year :
- 2018
- Publisher :
- International Union of Crystallography (IUCr), 2018.
-
Abstract
- The first crystal structure of a type II Baeyer–Villiger monooxygenase reveals a different ring orientation of its FMN cofactor compared with other related bacterial luciferase-family enzymes.<br />The three-dimensional structures of the native enzyme and the FMN complex of the overexpressed form of the oxygenating component of the type II Baeyer–Villiger 3,6-diketocamphane monooxygenase have been determined to 1.9 Å resolution. The structure of this dimeric FMN-dependent enzyme, which is encoded on the large CAM plasmid of Pseudomonas putida, has been solved by a combination of multiple anomalous dispersion from a bromine crystal soak and molecular replacement using a bacterial luciferase model. The orientation of the isoalloxazine ring of the FMN cofactor in the active site of this TIM-barrel fold enzyme differs significantly from that previously observed in enzymes of the bacterial luciferase-like superfamily. The Ala77 residue is in a cis conformation and forms a β-bulge at the C-terminus of β-strand 3, which is a feature observed in many proteins of this superfamily.
Details
- ISSN :
- 20597983
- Volume :
- 74
- Database :
- OpenAIRE
- Journal :
- Acta Crystallographica Section D Structural Biology
- Accession number :
- edsair.doi.dedup.....e6aa843ea99d761ede5c50e0c6b6954c