| DOI | Resolve DOI: https://doi.org/10.1107/S1399004715017939 |
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| Author | Search for: Isupov, Michail N.; Search for: Schröder, Ewald; Search for: Gibson, Robert P.; Search for: Beecher, Jean; Search for: Donadio, Giuliana; Search for: Saneei, Vahid; Search for: Dcunha, Stephlina A.; Search for: Mcghie, Emma J.; Search for: Sayer, Christopher; Search for: Davenport, Colin F.; Search for: Lau, Peter C.1; Search for: Hasegawa, Yoshie; Search for: Iwaki, Hiroaki; Search for: Kadow, Maria; Search for: Balke, Kathleen; Search for: Bornscheuer, Uwe T.; Search for: Bourenkov, Gleb; Search for: Littlechild, Jennifer A. |
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| Affiliation | - National Research Council of Canada. Aquatic and Crop Resource Development
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| Format | Text, Article |
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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 1.9Å 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. |
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| Publication date | 2015 |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NPARC number | 21277391 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 88f501d5-fee4-460b-8197-d3e0e7182e20 |
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| Record created | 2016-03-09 |
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| Record modified | 2020-04-22 |
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