STRUCTURAL STUDIES OF SIR2 RIBOSYLATION INTERMEDIATES

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。 Sir2酶催化乙酰赖氨酸残基的脱乙酰化。此外，一些Sir2酶可以催化精氨酸侧链的ADP核糖化。Sir2介导的核糖化反应机制尚不清楚。为了了解Sir2酶如何催化精氨酸的核糖化，除了Sir2-乙酰精氨酸肽-NAD+外，我还在Sir2晶体中捕获了Sir2-核糖化精氨酸产物-NAD+，这是核糖化的米氏络合物。为了获得我们的力学研究所需要的高分辨率数据，我们建议使用BIOCARS X射线束线进行研究。

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. Sir2 enzymes catalyze the deacetylation of acetyl lysine residues. Additionally, some Sir2 enzymes can catalyze the ADP ribosylation of arginine side chains. The reaction mechanism of Sir2 mediated ribosylation is not known. To understand how Sir2 enzymes catalyze ribosylation of arginine, I have trapped a Sir2-ribosylated arginine product in Sir2 crystals in addition to Sir2-acetyl arginine peptide-NAD+, which is the Michaelis complex for ribosylation. In order to obtain high resolution data that is necessary for our mechanistic studies, we propose using the BIOCARS X-Ray beam lines for our studies.