E COLI CLASS IA RIBONUCLEOTIDE REDUCTASE (RNR) HOLOCOMPLEX

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。 核苷酸还原酶是细胞中脱氧核苷酸的唯一来源，因此对所有活细胞都是至关重要的。虽然存在多种类型的RNR，但人们对大肠杆菌I类酶已有广泛的研究。该反应需要两种蛋白质，活性部位含有？和自由基产生蛋白？该蛋白质为催化所需的活性部位提供了自由基。虽然这两个亚基的结构是已知的，但络合物中没有可用的结构，齐聚状态也不是很清楚。我们正试图获得一种复合体的结构，以开始解决迄今为止使用的生化和生物物理方法尚未解决的一些问题。

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. Ribonucleotide reductases are the sole source of deoxyribonucleotides in the cell and are thus vital for all living cells. While there are multiple classes of RNR's the E. coli class I enzyme has been extensively studied. The reaction requires two proteins, the active site containing ¿ and the radical generating protein ¿. The ¿ protein provides a radical to the active site of ¿, required for catalysis. While structures of the two subunits are known, there is no available structure of ¿ and ¿ in complex and the oligomerization state is not well known. We are attempting to obtain a structure of ¿ and ¿ in complex to begin to address some of the issues unresolved by biochemical and biophysical methods used so far.