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二磷酸腺苷部分不参与使用AppA的黄素腺嘌呤二核苷酸结构域的蓝光传感器中信号传导状态的结构变化。

Adenosine diphosphate moiety does not participate in structural changes for the signaling state in the sensor of blue-light using FAD domain of AppA.

作者信息

Masuda Shinji, Hasegawa Koji, Ono Taka-Aki

机构信息

Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama 226-5801, Japan.

出版信息

FEBS Lett. 2005 Aug 15;579(20):4329-32. doi: 10.1016/j.febslet.2005.06.069.

Abstract

A sensor of blue light using FAD (BLUF) protein is a flavin adenine dinucleotide (FAD) based new class blue-light sensory flavoprotein. The BLUF domain of AppA was reconstituted in vitro from apoprotein and flavin adenine dinucleotide, flavin adenine mononucleotide or riboflavin. The light-induced FTIR spectra of the domain reconstituted from various flavins and the 13C-labeled apoprotein showed that identical light-induced structural changes occur in both the flavin chromophore and protein for the signaling state in all of the reconstituted holoproteins. The results showed that an adenosine 5'-dinucleotide moiety is not required for signaling-state formation in a BLUF domain.

摘要

一种使用黄素腺嘌呤二核苷酸(FAD)的蓝光传感器(BLUF)蛋白是一种基于黄素腺嘌呤二核苷酸的新型蓝光感应黄素蛋白。AppA的BLUF结构域在体外由脱辅基蛋白与黄素腺嘌呤二核苷酸、黄素腺嘌呤单核苷酸或核黄素重构而成。由各种黄素和13C标记的脱辅基蛋白重构的结构域的光诱导傅里叶变换红外光谱表明,在所有重构的全蛋白中,黄素发色团和蛋白质在信号状态下都会发生相同的光诱导结构变化。结果表明,腺苷5'-二核苷酸部分对于BLUF结构域中信号状态的形成并非必需。

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