BACTERIAL CHEMOTAXIS: STRUCTURE OF CHEA AND REGULATION OF ITS ACTIVITY

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。 在细菌趋化过程中，配体与跨膜化学感受器的结合调节组氨酸激酶CheA的活性。CheA通过磷酸化反应调节剂CheY启动细胞质信号传导，CheY从膜扩散以调节鞭毛马达。受体如何调节CheA活性是理解原核生物信号转导的中心问题。 我们的目标是在分子上详细了解受体：激酶复合物如何传播信号，然后适应这些激发。为了做到这一点，我们通过脉冲ESR测量15- 65 A范围内的一组距离约束，以仅几埃的分辨率确定单个蛋白质及其结构域的结构。受体与CheA之间的相互作用需要偶联蛋白CheW的结合。 然而，CheW如何结合到CheA是未知的，因此我们的第一个目标是解决这个结构问题。

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. During bacterial chemotaxis ligand binding to transmembrane chemoreceptors regulates the activity of the histidine kinase CheA. CheA initiates cytoplasmic signaling by phosphorylating the response regulator CheY, which diffuses from the membrane to modulate the flagellar motor. How receptors regulate CheA activity is a central question in understanding prokaryotic signal transduction. We aim to understand in molecular detail how the receptor:kinase complexes propagate signals and then adapt to those excitations. In order to do so, we determine structures of the individual proteins and their domains with just a few angstrom resolution by measuring a set of distance constraints in the 15-65A range by pulsed ESR. The interactions between receptors and CheA require the binding of the coupling protein CheW. However how CheW binds to CheA was unknown, and thus our first goal was aimed at solving this structural problem.