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首页> 外文期刊>Crystallography reports >Preparation of the crystal complex of phosphopantetheine adenylyltransferase from mycobacterium tuberculosis with coenzyme A and investigation of its three-dimensional structure at 2.1-? resolution
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Preparation of the crystal complex of phosphopantetheine adenylyltransferase from mycobacterium tuberculosis with coenzyme A and investigation of its three-dimensional structure at 2.1-? resolution

机译：用辅酶A从结核分枝杆菌中制备磷酸泛酸腺苷酸基转移酶的晶体配合物，并研究其在2.1-β处的三维结构。解析度

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摘要

Recombinant phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis (PPAT Mt), which was produced by a high-producing strain and purified to 99%, was used for the crystal growth of the complex of the enzyme with coenzyme A (CoA). Crystals suitable for X-ray diffraction study were obtained by cocrystallization. The crystals belong to sp. gr. R32 and have the unit-cell parameters a = b = 98.840 ?, c = 112.880 ?, α = β = 90.00°, and γ = 120.00°. The three-dimensional structure of the complex was determined based on X-ray diffraction data collected from the crystals to 2.1 ? resolution and refined to Rf = 22.7% and Rfree = 25.93%. Active-site bound coenzyme A was found, and its nearest environment was described. The conformational changes of the enzyme due to ligand binding were revealed. The binding of CoA by tuberculosis phosphopantetheine adenylyltransferase was characterized by comparing the structures of the title complex to a similar complex of PPAT from E. coli (PPAT Ec).
机译：通过高产菌株生产并纯化至99％的重组结核分枝杆菌磷酸泛泛素腺苷酸转移酶（PPAT Mt）用于该酶与辅酶A（CoA）的复合物的晶体生长。通过共结晶获得适合于X射线衍射研究的晶体。晶体属于sp。 gr。 R32的单位晶胞参数为a ＝ b ＝98.840θ，c ＝112.880θ，α＝β＝ 90.00°，γ＝ 120.00°。配合物的三维结构是根据从晶体收集到的2.1λ的X射线衍射数据确定的。分辨率并精炼为Rf = 22.7％和Rfree = 25.93％。发现了活性位点结合的辅酶A，并描述了其最近的环境。揭示了由于配体结合而引起的酶的构象变化。通过比较标题复合物与大肠杆菌中PPAT的类似复合物（PPAT Ec）的结构来表征肺结核磷酸泛肽腺苷酸腺苷酸转移酶对CoA的结合。

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