4UWM
Type II Baeyer-Villiger monooxygenase.The oxygenating constituent of 3,6-diketocamphane monooxygenase from CAM plasmid of Pseudomonas putida in complex with FMN.
Summary for 4UWM
Entry DOI | 10.2210/pdb4uwm/pdb |
Descriptor | 3,6-DIKETOCAMPHANE 1,6 MONOOXYGENASE, FLAVIN MONONUCLEOTIDE, TETRAETHYLENE GLYCOL, ... (6 entities in total) |
Functional Keywords | oxidoreductase, biocatalysis |
Biological source | PSEUDOMONAS PUTIDA |
Total number of polymer chains | 2 |
Total formula weight | 86795.69 |
Authors | Isupov, M.N.,Schroeder, E.,Gibson, R.P.,Beecher, J.,Donadio, G.,Saneei, V.,Dcunha, S.,McGhie, E.J.,Sayer, C.,Davenport, C.F.,Lau, P.C.,Hasegawa, Y.,Iwaki, H.,Kadow, M.,Loschinski, K.,Bornscheuer, U.T.,Bourenkov, G.,Littlechild, J.A. (deposition date: 2014-08-12, release date: 2015-08-26, Last modification date: 2024-01-10) |
Primary citation | Isupov, M.N.,Schroder, E.,Gibson, R.P.,Beecher, J.,Donadio, G.,Saneei, V.,Dcunha, S.A.,Mcghie, E.J.,Sayer, C.,Davenport, C.F.,Lau, P.C.,Hasegawa, Y.,Iwaki, H.,Kadow, M.,Balke, K.,Bornscheuer, U.T.,Bourenkov, G.,Littlechild, J.A. 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. Acta Crystallogr.,Sect.D, 71:2344-, 2015 Cited by PubMed 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 β-bulge at the C-terminus of β-strand 3, which is a feature observed in many proteins of this superfamily. PubMed: 26527149DOI: 10.1107/S1399004715017939 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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