STRUCTURAL STUDIES OF AN ADENINE DNA GLYCOSYLASE, MUTY

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。 MutY是一种腺嘌呤DNA糖基化酶，其识别与8-氧代鸟嘌呤相对的腺嘌呤核碱基并催化底物2 '-脱氧腺苷的N-糖苷键的裂解。 虽然以前的X射线晶体学研究提供了重要的见解8-氧代鸟嘌呤识别MutY，底物腺嘌呤识别和催化机制，这种酶知之甚少，在很大程度上是由于使用的酶失活MutY。我们的计划旨在通过确定与其抑制剂DNA结合的催化活性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.