Crystallization and preliminary X-ray analysis of the catalase-peroxidase KatG from Burkholderia pseudomallei

被引:14
作者
Carpena, X
Switala, J
Loprasert, S
Mongkolsuk, S
Fita, I
Loewen, PC [1 ]
机构
[1] Univ Manitoba, Dept Microbiol, Winnipeg, MB R3T 2N2, Canada
[2] CSIC, Inst Mol Biol, ES-08034 Barcelona, Spain
[3] Chulabhorn Res Inst, Biotechnol Lab, Bangkok 10210, Thailand
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2002年 / 58卷
关键词
D O I
10.1107/S0907444902017869
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The bifunctional catalase-peroxidase KatG encoded by the katG gene of Burkholderia pseudomallei has a predicted subunit size of 81.6 kDa. It shows high sequence similarity to other catalase- peroxidases of bacterial, archaebacterial and fungal origin, including 64% identity to KatG from Mycobacterium tuberculosis and lesser sequence similarity to members of the plant peroxidase family. Crystals from this protein were grown in 16-20% PEG 4000, 20% 2-methyl-2,4-pentanediol and 0.1 M sodium citrate pH 5.6 by the hanging-drop vapour-diffusion method at 293 K. These crystals diffracted beyond 1.8 Angstrom resolution and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 100.9, b = 115.6, c = 175.2 Angstrom. The data are consistent with either a monomer or a dimer in the crystal asymmetric unit.
引用
收藏
页码:2184 / 2186
页数:3
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