E COLI CLASS IA RIBONUCLEOTIDE REDUCTASE (RNR) HOLOCOMPLEX

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。子项目和 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。列出的机构是 中心，不一定是研究者的机构。 核糖核苷酸还原酶是细胞中脱氧核糖核苷酸的唯一来源，因此对所有活细胞至关重要。虽然有多个类别的RNR的E。大肠杆菌I类酶已被广泛研究。该反应需要两种蛋白质，活性位点包含<$和自由基生成蛋白<$。蛋白质提供了一个自由基的活性位点的催化，需要。虽然这两个亚基的结构是已知的，但在复合物中没有可利用的结构，并且寡聚化状态也不是很清楚。我们正试图获得一个复杂的结构，开始解决一些尚未解决的问题，生物化学和生物物理方法使用至今。

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.