INTERACTIONS BETWEEN PHOSPHO-ACCEPTING AND KINASE DOMAIN OF ECOLI CHEA

大肠杆菌 CHEA 磷酸接受结构域和激酶结构域之间的相互作用

• 批准号: 8364039
• 负责人: JAYA BHATNAGAR
• 金额: $ 0.05万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-09-01 至 2012-08-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8364039
• 关键词: Escherichia coli Proteins; Freedom; Funding; Grant; Histidine; National Center for Research Resources; Phosphotransferases; Principal Investigator; Research; Research Infrastructure; Resources; Source; Technology; United States National Institutes of Health; Work; cost; inorganic phosphate; protein-histidine kinase; research study

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. The kinase domain P4, transfers a phosphate group to the conserved histidine residue in the P1 domain of histidine kinase CheA. In this work we aim to determine the interaction between these two domains. Previous experiments have established that P1 domains are widely separated from each other and have considerable degree of freedom. In order to resolve the associated long distances, we use deuterated proteins from E.coli.

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。 激酶结构域P4将磷酸基团转移到组氨酸激酶CheA的P1结构域中的保守组氨酸残基。在这项工作中，我们的目标是确定这两个域之间的相互作用。以前的实验已经确定，P1域是广泛的相互分离，并有相当大的自由度。为了解决相关的长距离，我们使用来自大肠杆菌的氘代蛋白质。