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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallization and preliminary X-ray crystallographic analysis of aspartate 1-decarboxylase from Helicobacter pylori.
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Crystallization and preliminary X-ray crystallographic analysis of aspartate 1-decarboxylase from Helicobacter pylori.

机译：结晶和初步的x射线天冬氨酸盐晶体分析1-decarboxylase幽门螺杆菌。

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摘要

Aspartate 1-decarboxylase (PanD) catalyzes the alpha-decarboxylation of L-aspartate in the major route of beta-alanine production for pantothenate biosynthesis in bacteria. Pantothenate is synthesized in microorganisms, plants and fungi but not in animals and thus the enzymes of its biosynthetic pathway are potential targets for developing agents against these organisms. PanD from the pathogenic bacterium Helicobacter pylori has been overexpressed in Escherichia coli and crystallized using sodium formate as a precipitant. Crystals diffracted to better than 1.5 A Bragg spacing upon exposure to synchrotron X-rays. Diffraction data to 1.55 A have been collected from a crystal grown in the presence of the substrate analogue isoasparagine. The crystal belongs to the tetragonal space group I422, with unit-cell parameters a = b = 81.83, c = 93.78 A. The asymmetric unit contains one subunit of PanD, with a corresponding crystal volume per protein mass (V(M)) of 2.85 A(3) Da(-1) and a solvent content of 56.8%.
机译：天冬氨酸1-decarboxylase (PanD)催化alpha-decarboxylation L-aspartate的专业泛酸盐beta-alanine生产路线生物合成的细菌。合成在微生物、植物和真菌但不是在动物身上,因此酶的生物合成途径是潜在的目标对这些生物发展代理。幽门螺杆菌致病细菌在大肠杆菌和使用甲酸钠的结晶沉淀剂。布喇格间距在1.5同步x射线。从晶体生长在收集的存在底物模拟isoasparagine。属于正方空间群I422,晶胞参数a = b = 81.83, c = 93.78。PanD的不对称单元包含一个亚基,与一个相应的水晶卷/蛋白质质量(V (M))(3)达2.85(1)和溶剂内容的56.8%。

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