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

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。子项目及 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。 在大肠在大肠杆菌中，Min系统（MinD、MinD和MinE）通过将Z环组装限制在中间细胞位置来空间调节细胞分裂。MinD是一种膜相关ATP酶，是ATP酶大家族的一部分。这些包括Par蛋白和固氮酶铁蛋白家族。在FtsZ（微管蛋白同源物）之后，MinD是细胞分裂机制中最高度保守的组分。在ATP的存在下，MinD二聚化，结合到膜上并招募MinC。MinD与MinC结合，抑制细胞分裂。 与它们的功能一致，已经发现min系统从细胞极到细胞极振荡。 MinD ATP酶对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中间细胞。显然，确定MinD的活性ATP依赖性二聚体形式的结构将提供对这一重要分子的功能作用的重要见解。以前的MinD相关蛋白质的结构是单体从Escherichia sp.因此，生物学相关的ATP依赖性二聚体结构是未知的。 这些古细菌蛋白与E.大肠杆菌蛋白质（

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 (