STRUCTURAL STUDIES OF AN ADENINE DNA GLYCOSYLASE, MUTY

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。 MutY是一种腺嘌呤DNA糖基酶，它识别腺嘌呤核苷酸碱基，与8-氧鸟嘌呤相反，并催化底物2‘-脱氧腺苷的N-糖苷键的断裂。虽然先前的X射线结晶学研究为MutY识别8-氧鸟嘌呤提供了重要的见解，但这种酶对底物腺嘌呤的识别和催化机制尚不清楚，这在很大程度上是因为使用了酶活性不高的MutY。我们的计划旨在通过确定与其抑制剂DNA结合的具有催化活性的MutY的X射线结构来阐明这些机制。

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. MutY is an adenine DNA glycosylase that recognizes adenine nucleobase opposite 8-oxoguanine and catalyzes the cleavage of the N-glycosidic bond of the substrate 2'-deoxyadenosine. Although the previous X-ray crystallographic study provided significant insights into 8-oxoguanine recognition by MutY, the substrate adenine recognition and catalysis mechanisms by this enzyme are poorly understood, due in significant part to use of an enzymatically inactive MutY. Our program aims to shed light into these mechanisms by determining an X-ray structure of a catalytically active MutY bound to its inhibitor DNA.