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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 DOI10.2210/pdb4uwm/pdb
Descriptor3,6-DIKETOCAMPHANE 1,6 MONOOXYGENASE, FLAVIN MONONUCLEOTIDE, TETRAETHYLENE GLYCOL, ... (6 entities in total)
Functional Keywordsoxidoreductase, biocatalysis
Biological sourcePSEUDOMONAS PUTIDA
Total number of polymer chains2
Total formula weight86795.69
Authors
Primary citationIsupov, 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: 26527149
DOI: 10.1107/S1399004715017939
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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数据于2025-06-25公开中

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