STRUCTURE DETERMINATION OF LOV/LUXR PROTEIN FROM ERYTHOBACTER LITORALIS

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 有必要确定细菌内所含的各种光感受器的生理意义和分子特征。我们正在研究一个假定的光感受器从Erythobactor litoralis，被认为是在群体感应中发挥作用。这种222个氨基酸的蛋白质含有两个结构域：结合黄素单核苷酸（FMN）发色团的LOV（光、氧和电压）结构域和螺旋-转角-螺旋转录因子结构域（LuxR）。到目前为止，晶体条件已经确定，最近在瑞士光源（SLS）的测试运行期间获得了衍射至3.5埃的黄色大板晶体。除了深入了解细菌如何响应其环境以维持生命外，确定包含LOV结构域的蛋白质的结构还可以导致药物设计，从而使免疫受损个体的群体淬灭成为可能。

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.