STRUCTURE DETERMINATION OF LOV/LUXR PROTEIN FROM ERYTHOBACTER LITORALIS

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 有必要确定细菌中包含的各种光感受器的生理意义和分子特征。我们正在研究一种可能来自斜纹红毛虫的光感受器，该感受器被认为在群体感应中发挥作用。这个222个氨基酸的蛋白质包含两个结构域：一个与黄素单核苷酸(FMN)发色团结合的LOV(光、氧和电压)结构域，以及一个螺旋-转角-螺旋转录因子结构域(LuxR)。到目前为止，已经确定了晶体条件，最近在瑞士光源(SLS)的试运行中获得了衍射到3.5埃的黄色大片晶体。除了了解细菌如何对环境做出反应以维持生命外，确定包含蛋白质的LOV结构域的结构还可以导致药物设计，使免疫受损的个体能够进行法定人数猝灭。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. There is a need to determine the physiological significance and molecular characterization of various photoreceptors contained within bacteria. We are studying a putative photoreceptor from Erythobactor litoralis that is thought to play a role in quorum sensing. This 222 amino acid protein contains two domains: an LOV (light, oxygen, and voltage) domain which binds a flavin mononucleotide (FMN) chromophore, and a helix-turn-helix transcription factor domain (LuxR). So far, crystal conditions have been determined and yellow large plate crystals have recently been obtained diffracting to 3.5 Angstroms during a test run at the Swiss Light Source (SLS). In addition to gaining insight about how bacteria respond to their environment in order to maintain life, determining the structure of LOV domain containing proteins can lead to drug design enabling quorum quenching in immuno-compromised individuals.