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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Structure of isochorismate synthase DhbC from Bacillus anthracis
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Structure of isochorismate synthase DhbC from Bacillus anthracis

机译：炭疽芽孢杆菌等渗硫酸合酶DhbC的结构

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摘要

The isochorismate synthase DhbC from Bacillus anthracis is essential for the biosynthesis of the siderophore bacillibactin by this pathogenic bacterium. The structure of the selenomethionine-substituted protein was determined to 2.4 angstrom resolution using single-wavelength anomalous diffraction. B. anthracis DhbC bears the strongest resemblance to the Escherichia coli isochorismate synthase EntC, which is involved in the biosynthesis of another siderophore, namely enterobactin. Both proteins adopt the characteristic fold of other chorismate-utilizing enzymes, which are involved in the biosynthesis of various products, including siderophores, menaquinone and tryptophan. The conservation of the active-site residues, as well as their spatial arrangement, suggests that these enzymes share a common Mg2+-dependent catalytic mechanism.
机译：炭疽芽孢杆菌的等渗酸合酶DhbC对于这种病原菌生物合成铁载体细菌的作用至关重要。使用单波长反常衍射将硒甲硫氨酸取代的蛋白的结构确定为2.4埃分辨率。炭疽芽孢杆菌DhbC与大肠埃希氏杆菌等碳酸盐合酶EntC最相似，后者参与另一铁载体，即肠杆菌素的生物合成。两种蛋白质均具有其他利用分支酸盐的酶的特征性折叠，这些酶参与了多种产物的生物合成，包括铁载体，甲萘醌和色氨酸。活性位点残基的保守性及其空间排列表明，这些酶具有共同的Mg2 +依赖性催化机制。

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