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新鞘氨醇菌KA1咔唑1,9a-双加氧酶末端加氧酶的结晶及初步X射线衍射研究

Crystallization and preliminary X-ray diffraction studies of a terminal oxygenase of carbazole 1,9a-dioxygenase from Novosphingobium sp. KA1.

作者信息

Umeda Takashi, Katsuki Junichi, Ashikawa Yuji, Usami Yusuke, Inoue Kengo, 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. 2010 Nov 1;66(Pt 11):1480-3. doi: 10.1107/S1744309110034949. Epub 2010 Oct 28.

DOI:10.1107/S1744309110034949
PMID:21045300
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3001653/
Abstract

Carbazole 1,9a-dioxygenase (CARDO) is the initial dioxygenase in the carbazole-degradation pathway of Novosphingobium sp. KA1. The CARDO from KA1 consists of a terminal oxygenase (Oxy), a putidaredoxin-type ferredoxin and a ferredoxin reductase. The Oxy from Novosphingobium sp. KA1 was crystallized at 277 K using the hanging-drop vapour-diffusion method with ammonium sulfate as the precipitant. Diffraction data were collected to a resolution of 2.1 Å. The crystals belonged to the monoclinic space group P2(1). Self-rotation function analysis suggested that the asymmetric unit contained two Oxy trimers; the Matthews coefficient and solvent content were calculated to be 5.9 Å(3) Da(-1) and 79.1%, respectively.

摘要

咔唑1,9a-双加氧酶(CARDO)是新鞘氨醇菌KA1咔唑降解途径中的初始双加氧酶。来自KA1的CARDO由一个末端加氧酶(Oxy)、一个恶臭假单胞菌型铁氧还蛋白和一个铁氧还蛋白还原酶组成。使用硫酸铵作为沉淀剂,通过悬滴气相扩散法在277 K下使新鞘氨醇菌KA1的Oxy结晶。收集了分辨率为2.1 Å的衍射数据。晶体属于单斜空间群P2(1)。自旋转函数分析表明,不对称单元包含两个Oxy三聚体;计算得出的马修斯系数和溶剂含量分别为5.9 Å(3) Da(-1)和79.1%。

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Crystallization and preliminary X-ray diffraction studies of a ferredoxin reductase component of carbazole 1,9a-dioxygenase from Novosphingobium sp. KA1.来自新鞘氨醇菌属KA1的咔唑1,9a-双加氧酶铁氧化还原蛋白还原酶组分的结晶及初步X射线衍射研究。
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