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首页> 外文期刊>Acta crystallographica. Section D, Biological crystallography. >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
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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

机译：3的补氧成分,6-diketocamphane单氧酶从凸轮假单胞菌的质粒putida:第II型的晶体结构Baeyer-Villiger单氧酶

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摘要

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 angstrom 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.
机译：本机的三维结构酶和过表达的FMN复杂II型的补氧组件的形式已被认定为1.9埃分辨率。这种结构的二聚的FMN-dependent酶,在大型凸轮质粒编码假单胞菌的putida,已经解决了多个反常色散的组合一个溴的水晶泡和分子替换使用细菌荧光素酶模型。取向的FMN异咯嗪环代数余子式TIM-barrel的活性部位折叠酶显著不同以前观察到细菌的酶luciferase-like总科。顺式构象,形成beta-bulge糖基的beta-strand 3,这是一个在许多蛋白质的功能观察总科。

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