来自食芳烃诺卡氏菌IC177的咔唑1,9a-双加氧酶铁氧化还原蛋白组分的结晶及初步晶体学分析
Crystallization and preliminary crystallographic analysis of the ferredoxin component of carbazole 1,9a-dioxygenase from Nocardioides aromaticivorans IC177.
作者信息
Inoue Kengo, Ashikawa Yuji, Usami Yusuke, Noguchi Haruko, Fujimoto Zui, Yamane Hisakazu, Nojiri Hideaki
机构信息
Biotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Oct 1;63(Pt 10):855-7. doi: 10.1107/S1744309107041437. Epub 2007 Sep 19.
Abstract
Carbazole 1,9a-dioxygenase (CARDO) catalyzes the dihydroxylation of carbazole by angular position (C9a) carbon bonding to the imino nitrogen and its adjacent C1 carbon. CARDO consists of a terminal oxygenase component and two electron-transfer components: ferredoxin and ferredoxin reductase. The ferredoxin component of carbazole 1,9a-dioxygenase from Nocardioides aromaticivorans IC177 was crystallized at 293 K using the hanging-drop vapour-diffusion method with ammonium sulfate as the precipitant. The crystals, which were improved by macroseeding, diffract to 2.0 A resolution and belong to space group P4(1)2(1)2.
摘要
咔唑-1,9a-双加氧酶（CARDO）通过角位（C9a）碳与亚氨基氮及其相邻的C1碳形成键合来催化咔唑的双羟基化反应。CARDO由一个末端加氧酶组分和两个电子传递组分组成：铁氧还蛋白和铁氧还蛋白还原酶。利用悬滴气相扩散法，以硫酸铵作为沉淀剂，对来自食芳烃诺卡氏菌IC177的咔唑-1,9a-双加氧酶的铁氧还蛋白组分在293 K下进行了结晶。通过宏观接种改善后的晶体，其衍射分辨率达到2.0 Å，属于空间群P4(1)2(1)2。
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