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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of the photoactive yellow protein reconstituted with caffeic acid at 1.16 A resolution.
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Structure of the photoactive yellow protein reconstituted with caffeic acid at 1.16 A resolution.

机译:黄色光活化的蛋白质的结构1.16重组与咖啡酸决议。

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摘要

A structural study is described of the photoactive yellow protein (PYP) reconstituted with the chromophore derivative 3,4-dihydroxycinnamic acid. The crystal structure of PYP reconstituted with this chromophore at 1.16 A resolution is reported in space group P6(5). This is the first high-resolution structure of a photoreceptor containing a modified chromophore. The introduction of an extra hydroxyl group in the native chromophore (i.e. p-coumaric acid) appears to perturb the structure of the hybrid yellow protein only slightly. The chromophore is bound by the protein in two different conformations, separated by a rotation of 180 degrees of the catechol ring. In combination with available spectroscopic data, it is concluded that the caffeic acid chromophore binds to the protein in a strained conformation, which leads to a faster ejection from the chromophore-binding pocket upon pB formation.
机译:结构性研究是光敏的描述黄色的蛋白质(PYP)重组发色团衍生物3,4-dihydroxycinnamic酸。用这个发色团在1.16一项决议在空间群P6(5)。高分辨率光感受器的结构包含修改后的发色团。引入一个额外的羟基自然发色团(即p-coumaric酸)出现扰乱的结构混合黄色蛋白质仅略。蛋白质在两个不同的构象,相隔180度的旋转儿茶酚戒指。光谱数据,结果表明,咖啡酸发色团结合的蛋白质紧张的构象,从而导致更快退出chromophore-binding口袋里pB的形成。

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