首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Crystallization and preliminary X-ray crystallographic analysis of MbtI a protein essential for siderophore biosynthesis in Mycobacterium tuberculosis
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Crystallization and preliminary X-ray crystallographic analysis of MbtI a protein essential for siderophore biosynthesis in Mycobacterium tuberculosis

机译:MbtI的结晶和初步X射线晶体学分析MbtI是结核分枝杆菌中铁载体生物合成所必需的蛋白质

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摘要

Mycobacterium tuberculosis, the causative agent of tuberculosis, depends on the secretion of salicylate-based siderophores called mycobactins for the acquisition of extracellular iron, which is essential for the growth and virulence of the bacterium. The protein MbtI is thought to be the isochorismate synthase enzyme responsible for the conversion of chorismate to isochorismate, the first step in the salicylate production required for mycobactin biosynthesis. MbtI has been overexpressed in Escherichia coli, purified and crystallized. The crystals diffract to a maximum resolution of 1.8 Å. They belong to space group P212121, with unit-cell parameters a = 51.8, b = 163.4, c = 194.9 Å, consistent with the presence of either two, three or four molecules in the asymmetric unit.
机译:结核分枝杆菌是结核的病原体,取决于水杨酸酯基铁载体的分泌,称为分支杆菌素,用于获得细胞外铁,这对于细菌的生长和毒力至关重要。 MbtI蛋白被认为是异丁烯酸合成酶,负责将分支酸转化为异丁烯酸,这是分枝杆菌素生物合成所需的水杨酸酯生产的第一步。 MbtI已在大肠杆菌中过表达,纯化和结晶。晶体衍射到最大分辨率为1.8Å。它们属于空间群P212121,单位细胞参数a = 51.8,b = 163.4,c = 194.9Å,与不对称单元中存在两个,三个或四个分子一致。

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