STRUCTURAL CHARACTERIZATION OF THE ATP-DEPENDENT DIMER FORM OF BACTERIAL SEGEGRA

细菌 SEGEGRA ATP 依赖性二聚体形式的结构表征

• 批准号: 7722094
• 负责人: TODD HOLYOAK
• 金额: $ 0.11万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2008
• 资助国家: 美国
• 起止时间: 2008-03-01 至 2009-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7722094
• 关键词: ATP phosphohydrolase; Archaea; Archaeal Proteins; Behavior; Binding; Cell division; Cells; Computer Retrieval of Information on Scientific Projects Database; Escherichia coli; Escherichia coli Proteins; Family; Funding; Grant; Homologous Gene; Institution; Localized; Location; Masks; Membrane; Mind; Mining; Proteins; Recruitment Activity; Research; Research Personnel; Resources; Role; Site; Source; Structure; System; Tubulin; United States National Institutes of Health; dimer; insight; monomer; nitrogenase reductase

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. In E. coli the Min system (MinD, MinD and MinE) spatially regulates cell division by restricting Z ring assembly to a midcell location. MinD is a membrane associated ATPase, which is part of a larger family of ATPases. These include the family of Par proteins and nitrogenase iron proteins. After FtsZ (a tubulin homologue), MinD is the most highly conserved component of the cell division machinery. In the presence of ATP, MinD dimerizes, binds to the membrane and recruits MinC. MinD binds to MinC inhibiting cell division. Consistent with their function, the min system has been found to oscillate from cell pole to cell pole. The MinD ATPase is critical to the oscillation of the Min proteins. It has been proposed that this behavior masks potential division sites and localizes the cell division machinery to midcell. Clearly the determination of the structure of the active ATP-dependent dimer form of MinD will provide significant insight into the functional role of this important molecule. Previous structures of MinD related proteins are monomers from Archaea sp. Therefore the biologically relevant ATP dependent dimer structure is unknown. These archaeal proteins have little homology to the E. coli protein (

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。子项目和 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以在其他 CRISP 条目中表示。列出的机构是 对于中心来说，它不一定是研究者的机构。 在大肠杆菌中，Min 系统（MinD、MinD 和 MinE）通过将 Z 环组装限制在细胞中部位置来空间调节细胞分裂。 MinD 是一种膜相关 ATP 酶，属于更大的 ATP 酶家族的一部分。这些包括 Par 蛋白和固氮酶铁蛋白家族。 MinD 是继 FtsZ（微管蛋白同源物）之后细胞分裂机制中最高度保守的组件。在 ATP 存在的情况下，MinD 二聚化，与膜结合并招募 MinC。 MinD 与 MinC 结合抑制细胞分裂。 与它们的功能一致，最小系统被发现在细胞极之间振荡。 MinD ATP 酶对于 Min 蛋白的振荡至关重要。有人提出，这种行为掩盖了潜在的分裂位点，并将细胞分裂机制定位于细胞中部。显然，MinD 活性 ATP 依赖性二聚体形式的结构测定将为了解这一重要分子的功能作用提供重要的见解。 MinD 相关蛋白的先前结构是来自古细菌的单体。因此，生物学相关的 ATP 依赖性二聚体结构未知。 这些古细菌蛋白与大肠杆菌蛋白几乎没有同源性（