Structure determination and domain interaction of the photochromic protein YtvA from Bacillus subtilis

光是植物和各种细菌的重要刺激因素。因此，这些生物发展了许多感光器，通常由一种蛋白质和一种有机辅因子组成，以感知不同波长的光。光感知的详细机制，即受体的“初级事件”和随后的连续构象变化，目前还知之甚少。本项目将研究枯草芽孢杆菌黄素结合蓝光感光体YtwA的结构和结构域相互作用。这种光感受器是一个双域蛋白，由一个LOV(光、氧、电压)结构域(含有黄素发色团)和一个STAS(硫酸盐转运蛋白抗Sigma因子拮抗剂)结构域组成。利用现代核磁共振技术，结合同位素标记，将确定YTVA的三维结构(目前尚未获得)，并将确定两个结构域之间的相互作用。因此，在生物学信号转导的初始过程中，从黑暗到发光(信号)状态发生的变化将被揭示。

Light is an important stimulus for plants and various bacteria. These organisms have therefore developed a number of photoreceptors, usually consisting of a protein and an organic cofactor, to sense light of different wavelengths. The detailed mechanism of light perception, i.e., the “primary event” and the consecutively following conformational changes of the receptor, are still only poorly understood. In this project the structure and domain interaction of the flavin-binding, blue-light photoceptor YtvA from Bacillus subtilis will be studied. This photoreceptor is a two-domain protein, consisting of a LOV (light, oxygen, voltage) domain (harboring a flavin chromophore) and a STAS (Sulphate Transporters AntiSigma-factor antagonist) domain. Utilizing modern NMR-techniques in conjunction with isotopelabeling, the three-dimensional structure of YtvA (which is not yet available) will be determined and the interactions between both domains will be identified. Thus the changes that occur during the transition from the dark into the illuminated (signaling) state as the initial process of signal transduction in biology will be revealed.