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。因此，这些生物体已经开发出许多光感受器，通常由蛋白质和有机辅因子组成，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”和随后的构象变化仍然知之甚少。在这个项目中的结构和结构域相互作用的黄素结合，蓝光光受体枯草芽孢杆菌YtvA将进行研究。这种光感受器是一种双结构域蛋白，由LOV（光、氧、电压）结构域（含有黄素发色团）和STAS（硫酸盐转运蛋白抗σ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示踪，YtvA的三维结构（尚未获得）将被确定，并将确定两个域之间的相互作用。因此，从黑暗到发光（信号）状态的转变过程中发生的变化，作为生物学中信号转导的初始过程将被揭示。

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.