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. Corrigendum
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. Corrigendum
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来自恶臭假单胞菌 CAM 质粒的 3,6-二酮莰烷单加氧酶的氧化成分：II 型 Baeyer-Villiger 单加氧酶的第一个晶体结构。
DOI：
10.1107/s205979831800150x
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发表时间：
2018
期刊：
影响因子：
--
通讯作者：
Isupov M
中科院分区：
文献类型：
--
作者：
Isupov M
天然酶和II型Baeyer-Villiger 3，6-二酮基双烷单加氧酶的氧化组分的过表达形式的FMN复合物的三维结构已被确定为1.9 μ m分辨率。 这种二聚体的FMN依赖的酶，这是编码的大CAM质粒的恶臭假单胞菌，已解决了由多个异常分散的溴晶体浸泡和分子置换使用细菌荧光素酶模型的组合。FMN辅因子的异咯嗪环在该TIM桶折叠酶的活性位点中的取向显著不同于先前在细菌类辅酶超家族的酶中观察到的取向。Ala 77残基呈顺式构象，并在β-链3的C-末端形成β-凸起，这是在该超家族的许多蛋白质中观察到的特征。
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 Å 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 β-bulge at the C-terminus of β-strand 3, which is a feature observed in many proteins of this superfamily.