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

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。所列机构为 中心，不一定是研究者的机构。 Acek是一种双功能激酶和磷酸酶，调节异柠檬酸脱氢酶（IDH）参与的旁路克雷布斯？周期这是在细菌中发现的第一个磷酸化系统，也是仅有的两个已知的Ser/Thr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个蛋白质中激酶和磷酸酶之间分子开关的结构基础。此外，我们最近获得了Acek和IDH之间的复合物晶体，这很可能是第一个与蛋白质底物的激酶复合物结构。 这种复杂的结构将为底物识别和活性调节提供新的思路。

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.