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首页> 外文期刊>Acta crystallographica. Section D, Structural biology. >The evolving story of AtzT, a periplasmic bindingprotein
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The evolving story of AtzT, a periplasmic bindingprotein

机译:周质的AtzT进化的故事

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Atrazine is an s-triazine-based herbicide that is used in many countries aroundthe world in many millions of tons per year. A small number of organisms, suchas Pseudomonas sp. strain ADP, have evolved to use this modified s-triazine as afood source, and the various genes required to metabolize atrazine can be foundon a single plasmid. The atomic structures of seven of the eight proteins involvedin the breakdown of atrazine by Pseudomonas sp. strain ADP have beendetermined by X-ray crystallography, but the structures of the proteins requiredby the cell to import atrazine for use as an energy source are still lacking. Thestructure of AtzT, a periplasmic binding protein that may be involved in thetransport of a derivative of atrazine, 2-hydroxyatrazine, into the cell formineralization, has now been determined. The structure was determined bySAD phasing using an ethylmercury phosphate derivative that diffracted X-raysto beyond 1.9 A resolution. 'Native' (guanine-bound) and 2-hydroxyatrazine-bound structures were also determined to high resolution (1.67 and 1.65 A,respectively), showing that 2-hydroxyatrazine binds in a similar way to thepurportedly native ligand. Structural similarities led to the belief that it may bepossible to evolve AtzT from a purine-binding protein to a protein that can bindand detect atrazine in the environment.
机译:阿特拉津是一种s-triazine-based除草剂在世界各地的许多国家在许多使用每年数百万吨。生物,如假单胞菌sp.应变ADP,使用这个修改s-triazine进化吗afood源和所需的各种基因代谢可以末端一个阿特拉津质粒。八个蛋白质分解的侵袭阿特拉津的假单胞菌sp.应变ADP做出的x射线晶体学,但是requiredby细胞结构的蛋白质进口阿特拉津作为能量来源仍然缺乏。周质的结合蛋白可能参与其中在阿特拉津的导数,thetransport2-hydroxyatrazine,进入细胞formineralization,现在已经确定。结构是决定bySAD逐步使用氯化乙基磷酸衍生物衍射X-raysto超出1.9一项决议。(guanine-bound)和2-hydroxyatrazine-bound结构也决心要高分辨率(分别为1.67和1.65),表明2-hydroxyatrazine绑定在一个相似的thepurportedly本机配体的方法。相似性导致相信它可能从purine-binding)来说AtzT发展蛋白质蛋白质bindand检测阿特拉津的环境。

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