The oxygenating constituent of 3,6-diketocamphane monooxygenase from the CAM plasmid of Pseudomonas putida: the first crystal structure of a type II Baeyer-Villiger monooxygenase.
Isupov, MN; Schröder, E; Gibson, RP; et al.Beecher, J; Donadio, G; Saneei, V; Dcunha, SA; McGhie, EJ; Sayer, Christopher; Davenport, CF; Lau, PC; Hasegawa, Y; Iwaki, H; Kadow, M; Balke, K; Bornscheuer, UT; Bourenkov, G; Littlechild, JA
Date: 1 November 2015
Journal
Acta Crystallographica Section D: Biological Crystallography
Publisher
International Union of Crystallography
Publisher DOI
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Abstract
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 ...
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.
Biosciences - old structure
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