5aec | pdb_00005aec

Type II Baeyer-Villiger monooxygenase.The oxygenating constituent of 3,6-diketocamphane monooxygenase from CAM plasmid of Pseudomonas putida in complex with FMN.

spinqualitylabelsall models 5aec, resolution 1.93Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5aec is a 2 chain structure with sequence from Pseudomonas putida. This structure supersedes the now removed PDB entry 2wgk. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.93Å Ligands: CL, GOL, PIN, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 36DKM_PSEPU Involved in the degradation and assimilation of (-)-camphor, which allows P.putida strain NCIMB 10007 to grow on this enantiomer of camphor as the sole carbon source (PubMed:8515237). Catalyzes the FMNH(2)-dependent lactonization of 3,6-diketocamphane via a Baeyer-Villiger oxidation to produce the unstable lactone 5-oxo-1,2-campholide with (S,S) configuration, that presumably undergoes spontaneous hydrolysis to form 2-oxo-Delta(3)-4,5,5-trimethylcyclopentenylacetate (PubMed:23524667). Is also able to convert (-)-camphor to the corresponding lactone in vitro (PubMed:23524667, PubMed:22286514, PubMed:8515237). Shows no conversion of (+)-camphor, (+)-fenchone, (-)-fenchone, and (+)-nopinone. Acts on other bicyclic ketones but very poorly on a few 2- and 4-substituted monocyclic ketones (PubMed:23524667). Publication Abstract from PubMed 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 A 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 beta-bulge at the C-terminus of beta-strand 3, which is a feature observed in many proteins of this superfamily. 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.,Isupov MN, Schroder E, Gibson RP, Beecher J, Donadio G, Saneei V, Dcunha SA, McGhie EJ, Sayer C, Davenport CF, Lau PC, Hasegawa Y, Iwaki H, Kadow M, Balke K, Bornscheuer UT, Bourenkov G, Littlechild JA Acta Crystallogr D Biol Crystallogr. 2015 Nov 1;71(Pt 11):2344-53. doi:, 10.1107/S1399004715017939. Epub 2015 Oct 31. PMID:26527149 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Monooxygenase 3D structures

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