STRUCTURE DETERMINATION OF LOV/LUXR PROTEIN FROM ERYTHOBACTER LITORALIS

滨红杆菌 LOV/LUXR 蛋白的结构测定

• 批准号: 8362161
• 负责人: Reginald McNulty
• 金额: $ 0.19万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-03-01 至 2012-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8362161
• 关键词: Amino Acids; Bacteria; Binding; Drug Design; Environment; Flavin Mononucleotide; Funding; Grant; Helix-Turn-Helix Motifs; Individual; Lead; Life; Light; Molecular; National Center for Research Resources; Oxygen; Photoreceptors; Physiological; Play; Principal Investigator; Proteins; Radiation; Research; Research Infrastructure; Resources; Role; Running; Source; Structure; Testing; United States National Institutes of Health; chromophore; cost; insight; luxR protein; quorum sensing; structural biology; transcription factor; voltage

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. 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.

这个子项目是许多利用资源的研究子项目之一 由NIH/NCRR资助的中心拨款提供。子项目的主要支持 而子项目的主要调查员可能是由其他来源提供的， 包括其它NIH来源。 列出的子项目总成本可能 代表子项目使用的中心基础设施的估计数量， 而不是由NCRR赠款提供给子项目或子项目工作人员的直接资金。 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。