Signal transduction in LOV and BLUF blue light photoreceptors.

该项目旨在获得新的光激活酶的结构信息含有黄素和视黄酸为基础的感光域。其主要目标是了解感光器的感知域和调节输出实体之间的耦合，任何合理的功能（重新）设计，以增加潜在的应用程序的先决条件。我们将专注于几个天然的光激活环化酶（PAC）的Astasia和Beggiatoa，光激活激酶（phototropins）的转板藻，和光调控的转录因子（Aureochrome）的Heterokontophytes的表达。此外，我们将致力于定制设计的合成系统，其中光传感器结构域中诱导的结构变化揭示了与所连接的输出结构域的调节蛋白的相互作用区域。我们将通过一个通用的HAMP结构域连接器，将研究充分的细菌环化酶与光敏的phoborhodopsin（SRII）合并，从而构建视紫红质环化酶嵌合体。所有功能性和光活化的蛋白质都将进行结晶筛选以确定结构。将在体外和体内详细研究结构特征蛋白质的酶，光谱和功能。

This project aims at obtaining new structural information on light-activated enzymes containing flavin- and retinal-based photoreceptor domains. The major goal is to understand the coupling between the sensing photoreceptor domains and the regulated output entities, a prerequisite for any rational (re)design of function to increase potential applications. We will focus on the expression of several natural light-activated cyclases (PAC) of Astasia and Beggiatoa, light-activated kinases (phototropins) of Mougeotia, and light-regulated transcription factors (Aureochromes) of Heterokontophytes. In addition, we will work on custom-designed synthetic systems where the structural changes induced in the photosensor domain unmask interaction regions with regulatory proteins of the attached output domain. We will engineer rhodopsin-cyclase chimera by merging well-studied bacterial cyclases with the light-sensitive phoborhodopsin (SRII) via a versatile HAMP domain linker. All proteins that are functional and light-activatable will be subjected to crystallization screens for structure determination. Structurally characterized proteins will be studied in detail enzymatically, spectroscopically and functionally in vitro and in vivo.