Crystallization and preliminary X-ray diffraction studies of a ferredoxin reductase component of carbazole 1,9a-dioxygenase from Novosphingobium sp KA1

被引:5
|
作者
Umeda, Takashi [1 ]
Katsuki, Junichi [1 ]
Ashikawa, Yuji [1 ,2 ]
Usami, Yusuke [1 ]
Inoue, Kengo [1 ]
Noguchi, Haruko [1 ]
Fujimoto, Zui [3 ]
Yamane, Hisakazu [1 ]
Nojiri, Hideaki [1 ,4 ]
机构
[1] Univ Tokyo, Biotechnol Res Ctr, Profess Programme Agr Bioinformat, Bunkyo Ku, Tokyo 1138657, Japan
[2] RIKEN, Mol Signaling Res Team, Struct Physiol Res Grp, Harima Inst,SPring Ctr 8, Sayo, Hyogo 6795148, Japan
[3] Natl Inst Agrobiol Sci, Protein Res Unit, Tsukuba, Ibaraki 3058602, Japan
[4] Univ Tokyo, Profess Programme Agr Bioinformat, Bunkyo Ku, Tokyo 1138657, Japan
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2010年 / 66卷
关键词
NONHEME IRON OXYGENASE; CRYSTAL-STRUCTURE; ELECTRON-TRANSFER; DIOXYGENASE;
D O I
10.1107/S1744309110014491
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Carbazole 1,9a-dioxygenase (CARDO) is the initial enzyme of the carbazole-degradation pathway. The CARDO of Novosphingobium sp. KA1 consists of a terminal oxygenase, a putidaredoxin-type ferredoxin and a ferredoxin-NADH oxidoreductase (Red) and is classified as a class IIA Rieske oxygenase. Red from KA1 was crystallized at 278 K by the hanging-drop vapour-diffusion method using PEG 4000. The crystal diffracted to 1.58 angstrom resolution and belonged to space group P3(2), with unit-cell parameters a = b = 92.2, c = 78.6 angstrom, alpha = gamma = 90, beta = 120 degrees. Preliminary analysis of the X-ray diffraction data revealed that the asymmetric unit contained two Red monomers. The crystal appeared to be a merohedral twin, with a twin fraction of 0.32 and twin law (-h, -k, l).
引用
收藏
页码:712 / 714
页数:3
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