4RG3

Epsilon-caprolactone-bound crystal structure of cyclohexanone monooxygenase in the Tight conformation

4RG3 の概要

• エントリーDOI: 10.2210/pdb4rg3/pdb
• 関連するPDBエントリー: 3GWD 3GWF 3UCL 4RG4
• 分子名称: Cyclohexanone monooxygenase, FLAVIN-ADENINE DINUCLEOTIDE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (6 entities in total)
• 機能のキーワード: baeyer-villiger monooxygenase, baeyer-villiger oxidation, biocatalysis, flavoprotein, green chemistry, protein engineering, rossmann fold, oxidoreductase, fad, nadph, cyclohexanone, oxygen, cytosolic (bacterial)
• 由来する生物種: Rhodococcus sp. HI-31
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 62614.88

構造登録者

Yachnin, B.J.,Berghuis, A.M. (登録日: 2014-09-29, 公開日: 2014-10-15, 最終更新日: 2023-09-20)

主引用文献

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

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: 25265531
DOI: 10.1021/cb500442e

実験手法

X-RAY DIFFRACTION (1.94 Å)