Crystallization and preliminary diffraction studies of the C-terminal domain of the DipZ homologue from Mycobacterium tuberculosis

被引：5
|
作者：
Goldstone, D [1 ]
Baker, EN [1 ]
Metcalf, P [1 ]
机构：
[1] Univ Auckland, Sch Biol Sci, Auckland 1, New Zealand
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2005年 / 61卷
关键词：
D O I：
10.1107/S1744309105001909
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Protein disulfide-bond formation is poorly understood in the pathogenic bacterium Mycobacterium tuberculosis. Rv2874 is the M. tuberculosis homologue of the disulfide-bond electron transporter DsbD from Escherichia coli. Both proteins share a core central transmembrane domain and a C-terminal thioredoxin domain. To investigate the possible role of Rv2874 in disulfide-bond formation in M. tuberculosis, the C-terminal domain of Rv2874 has been cloned, expressed, purified and crystallized. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 109.7, b = 118.3, c = 122.9 angstrom, and diffract to at least 3.0 angstrom.
引用
收藏
页码：243 / 245
页数：3
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