ACEK, A BIFUNCTIONAL KINASE/PHOSPHATASE, AND ITS COMPLEX WITH SUBSTRATE

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。 AceK是一种双功能的激酶和磷酸酶，调节参与Krebs？旁路的异柠檬酸脱氢酶(IDH)。周而复始。这是第一个在细菌中发现的磷酸化系统，也是仅有的两个已知的丝氨酸/苏氨酸磷酸化系统之一。AceK可能具有一个新的结构折叠，Acek的结构可能揭示了单一蛋白质中激酶和磷酸酶之间分子切换的结构基础。此外，我们最近还获得了Acek和IDH之间的复合晶体，这很可能是第一个以蛋白质为底物的激酶复合结构。这种复杂的结构将为底物识别和活性调控提供新的线索。

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. Acek is a bifunctional kinase and phosphatase, which regulates isocitrate dehydrogenase (IDH) involved in a bypass of Krebs? cycle. This was the first phosphorylation system to be identified in bacteria, and is one of the only two known Ser/Thr phosphorylation systems. AceK may possess a novel structural fold and the structure of Acek may reveal the structural basis of molecular switch between kinase and phosphatase within a single protein. Furthermore, we have recently obtained a complex crystal between Acek and IDH, which may well be the first kinase complex structure with protein substrate. This complex structure will shed new lights on the substrate recognition and activity regulation.