4RG4
Epsilon-caprolactone-bound crystal structure of cyclohexanone monooxygenase in the Loose conformation
Summary for 4RG4
| Entry DOI | 10.2210/pdb4rg4/pdb |
| Related | 3GWD 3GWF 3UCL 4RG3 |
| Descriptor | Cyclohexanone monooxygenase, FLAVIN-ADENINE DINUCLEOTIDE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (6 entities in total) |
| Functional Keywords | baeyer-villiger monooxygenase, baeyer-villiger oxidation, biocatalysis, flavoprotein, green chemistry, protein engineering, rossmann fold, oxidoreductase, fad, nadph, cyclohexanone, oxygen, glutaraldehyde crystal cross-linking, cytosolic (bacterial) |
| Biological source | Rhodococcus sp. HI-31 |
| Total number of polymer chains | 1 |
| Total formula weight | 62651.94 |
| Authors | Yachnin, B.J.,Berghuis, A.M. (deposition date: 2014-09-29, release date: 2014-10-15, Last modification date: 2023-09-20) |
| Primary citation | Yachnin, B.J.,McEvoy, M.B.,MacCuish, R.J.,Morley, K.L.,Lau, P.C.,Berghuis, A.M. Lactone-bound structures of cyclohexanone monooxygenase provide insight into the stereochemistry of catalysis. Acs Chem.Biol., 9:2843-2851, 2014 Cited by PubMed Abstract: The Baeyer-Villiger monooxygenases (BVMOs) are microbial enzymes that catalyze the synthetically useful Baeyer-Villiger oxidation reaction. The available BVMO crystal structures all lack a substrate or product bound in a position that would determine the substrate specificity and stereospecificity of the enzyme. Here, we report two crystal structures of cyclohexanone monooxygenase (CHMO) with its product, ε-caprolactone, bound: the CHMO(Tight) and CHMO(Loose) structures. The CHMO(Tight) structure represents the enzyme state in which substrate acceptance and stereospecificity is determined, providing a foundation for engineering BVMOs with altered substrate spectra and/or stereospecificity. The CHMO(Loose) structure is the first structure where the product is solvent accessible. This structure represents the enzyme state upon binding and release of the substrate and product. In addition, the role of the invariant Arg329 in chaperoning the substrate/product during the catalytic cycle is highlighted. Overall, these data provide a structural framework for the engineering of BVMOs with altered substrate spectra and/or stereospecificity. PubMed: 25265531DOI: 10.1021/cb500442e PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.51 Å) |
Structure validation
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