STRUCTURAL PARAMETERS INVOLVED IN METAL RECOGNITION

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 拟议的XAS实验是一个项目的一部分，该项目旨在研究大自然如何设计蛋白质，从细胞中存在的所有金属中识别一种金属(或一小部分金属)，并产生特定的生物反应。之所以选择参与大肠杆菌和幽门螺杆菌中镍运输的蛋白质，是因为希望检查整个运输系统(镍运输模式简单)，以了解特定金属识别的一般特征，并且因为抗生素策略可能会干扰细菌的镍运输。XAS为研究与金属转运体、金属配位体和金属调节剂结合的同源和非同源金属离子的结构提供了主要的结构工具。

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. The proposed XAS experiments are part of a project designed to examine how nature designs proteins to recognize one metal (or small group of metals) from all the metals present in cells, and generate specific biological responses. Proteins involved in nickel trafficking in E. coli and H. pylori were chosen because of the desire to examine an entire trafficking system (simplicity of the nickel traffic pattern) in order to understand the general features of specific metal recognition, and because of the potential for antibiotic strategies involving interference with bacterial nickel trafficking. XAS provides the main structural tool for examining the structure of cognate and non-cognate metal ions bound to metallotransporters, metallochaperones, and metalloregulators.