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来自类鼻疽伯克霍尔德菌的过氧化氢酶-过氧化物酶KatG的结晶及初步X射线分析

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

作者信息

Carpena Xavier, Switala Jack, Loprasert Suvit, Mongkolsuk Skorn, Fita Ignacio, Loewen Peter C

机构信息

Institut de Biología Molecular de Barcelona CSIC, Jordi-Girona 18-26, 08034 Barcelona, Spain.

出版信息

Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):2184-6. doi: 10.1107/s0907444902017869. Epub 2002 Nov 23.

DOI:10.1107/s0907444902017869
PMID:12454496
Abstract

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 A 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 A. The data are consistent with either a monomer or a dimer in the crystal asymmetric unit.

摘要

由伯克霍尔德菌属假鼻疽杆菌的katG基因编码的双功能过氧化氢酶-过氧化物酶KatG预测亚基大小为81.6 kDa。它与细菌、古细菌和真菌来源的其他过氧化氢酶-过氧化物酶具有高度的序列相似性,包括与结核分枝杆菌的KatG有64%的同一性,与植物过氧化物酶家族成员的序列相似性较低。该蛋白的晶体通过悬滴气相扩散法在293 K下于16 - 20%聚乙二醇4000、20% 2-甲基-2,4-戊二醇和0.1 M柠檬酸钠pH 5.6中生长。这些晶体的衍射分辨率超过1.8 Å,属于空间群P2(1)2(1)2(1),晶胞参数a = 100.9,b = 115.6,c = 175.2 Å。数据表明晶体不对称单元中可能是单体或二聚体。

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