3ucl | pdb_00003ucl

Cyclohexanone-bound crystal structure of cyclohexanone monooxygenase in the Rotated conformation

spinqualitylabelsall models 3ucl, resolution 2.36Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ucl is a 1 chain structure with sequence from Rhodococcus sp. hi-31. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CYH, FAD, NAP Related: 3gwf, 3gwd Gene: chnB, chnB1 (Rhodococcus sp. HI-31) Activity: Cyclohexanone monooxygenase, with EC number 1.14.13.22 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The Baeyer-Villiger monooxygenases (BVMOs) are a family of bacterial flavoproteins that catalyze the synthetically useful Baeyer-Villiger oxidation reaction. This involves the conversion of ketones into esters or cyclic ketones into lactones by introducing an oxygen atom adjacent to the carbonyl group. The BVMOs offer exquisite regio- and enantiospecificity while acting on a wide range of substrates. They use only NADPH and oxygen as co-substrates, and produce only NADP<sup>+</sup> and water as by-products, making them environmentally attractive for industrial purposes. Here, we report the first crystal structure of a BVMO, cyclohexanone monooxygenase (CHMO) from <italic>Rhodococcus</italic> sp. HI-31 in complex with its substrate, cyclohexanone, as well as NADP<sup>+</sup> and FAD, to 2.4 A resolution. This structure shows a drastic rotation of the NADP<sup>+</sup> cofactor in comparison to previously reported NADP<sup>+</sup>-bound structures, as the nicotinamide moiety is no longer positioned above the flavin ring. Instead, the substrate, cyclohexanone, is found at this location, in an appropriate position for the formation of the Criegee intermediate. The rotation of NADP<sup>+</sup> permits the substrate to gain access to the reactive flavin peroxyanion intermediate while preventing it from diffusing out of the active site. The structure thus reveals the conformation of the enzyme during the key catalytic step. CHMO is proposed to undergo a series of conformational changes to gradually move the substrate from the solvent, via binding in a solvent excluded pocket that dictates the enzyme's chemospecificity, to a location above the flavin-peroxide adduct where catalysis occurs. The substrate-bound crystal structure of a Baeyer-Villiger monooxygenase exhibits a Criegee-like conformation.,Yachnin BJ, Sprules T, McEvoy MB, Lau PC, Berghuis AM J Am Chem Soc. 2012 Apr 16. PMID:22506764 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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