AN INDUCED-FIT MODEL FOR LANTIBIOTIC AUTOIMMUNITY

这个子项目是利用由NIH/NCRR资助的中心拨款提供的资源的许多研究子项目之一。子项目和调查员(PI)可能从另一个NIH来源获得了主要资金，因此可能会出现在其他CRISE条目中。列出的机构是针对中心的，而不一定是针对调查员的机构。革兰氏阳性细菌乳酸乳杆菌产生l抗生素乳链菌素，这是一种膜孔形成剂，针对其他革兰氏阳性生物中的脂类II。为了保护自己不受这种抗生素的腐蚀性，乳酸乳杆菌产生一种名为NISI的蛋白质，它通过结合和灭活l抗生素来保护自己免受造孔剂Nisin的伤害。我们从以前的研究中得知，当NISI不与其同源底物Nisin结合时，NISI是无序的。利用光谱旋光法，我们希望证明NISI在与Nisin结合后变得有序。

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 gram-positive bacterium L. lactis produces the lantibiotic nisin which is a membrane pore forming agent that targets lipid II in other gram-positive organisms. To protect itself from the caustic nature of this lantibiotic, L. lactis produces a protein called NisI which protects itself from the pore-forming agent nisin by binding and inactivating the lantibiotic. We know from previous studies that NisI is disordered when not bound to its cognate substrate nisin. Using spectropolarimetry, we hope to show that NisI becomes ordered upon binding to nisin.