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

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DOIResolve DOI: http://doi.org/10.1107/S1399004715017939
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TypeArticle
Journal titleActa Crystallographica Section D: Biological Crystallography
ISSN0907-4449
Volume71
Pages23442353; # of pages: 10
AbstractThe 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 1.9Å 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.
Publication date
PublisherInternational Union of Crystallography
LanguageEnglish
AffiliationNational Research Council Canada (NRC-CNRC); Aquatic and Crop Resource Development
Peer reviewedYes
NPARC number21277391
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Record identifier88f501d5-fee4-460b-8197-d3e0e7182e20
Record created2016-03-09
Record modified2016-05-09
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