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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

DOI: 10.1107/S1399004715017939 DOI Help
PMID: 26527149 PMID Help

Authors: Mishail N. Isupov (University of Exeter) , Ewald Schröder (University of Exeter) , Robert P. Gibson (University of Exeter) , Jean Beecher (University of Exeter) , Giuliana Donadio (University of Exeter) , Vahid Saneei (University of Exeter) , Stephlina A. Dcunha (University of Exeter) , Emma J. Mcghie (University of Exeter) , Christopher Sayer (University of Exeter) , Colin F. Davenport (University of Exeter) , Peter C. Lau (National Research Council Canada) , Yoshie Hasegawa (Kansai University) , Hiroaki Iwaki (Kansai University) , Maria Kadow (Greifswald University) , Kathleen Balke (Greifswald University) , Uwe T. Bornscheuer (Greifswald University) , Gleb Bourenkov (Greifswald University) , Jennifer Littlechild (University of Exeter)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section D Biological Crystallography , VOL 71 (11) , PAGES 2344 - 2353

State: Published (Approved)
Published: November 2015
Diamond Proposal Number(s): 8889

Open Access Open Access

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 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 -bulge at the C-terminus of -strand 3, which is a feature observed in many proteins of this superfamily.

Journal Keywords: Fmn-Dependent Monooxygenase; Protein Structure; Industrial Biocatalysis.

Subject Areas: Biology and Bio-materials


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength)

Other Facilities: DESY