Department of Molecular and Cell Biology, QB3 Institute, University of California, Berkeley, CA 94720-3220, USA.
Curr Opin Struct Biol. 2009 Dec;19(6):650-7. doi: 10.1016/j.sbi.2009.10.017. Epub 2009 Nov 14.
Like eukaryotes, bacteria express receptor Ser/Thr protein kinases (STPKs) that initiate a wide variety of signaling networks. Recent biochemical and structural studies of the STPKs of Mycobacterium tuberculosis have revealed that bacterial and eukaryotic STPKs adopt common folds and share mechanisms of substrate recognition and regulation. Mycobacterial receptor STPKs are activated by dimerization through two distinct interfaces that promote activation-loop phosphorylation. The active STPKs phosphorylate diverse substrates within the bacterial cell, including other kinases as well as proteins involved in many central physiological processes. In the case of the FHA-domain protein, GarA, the unphosphorylated protein regulates primary metabolism, while phosphorylation mediates GarA autoinhibition. These studies have begun to define the activation mechanisms and the biological regulatory functions of the mycobacterial STPKs.
与真核生物一样，细菌表达受体丝氨酸/苏氨酸蛋白激酶（STPKs），这些激酶启动了各种各样的信号网络。最近对结核分枝杆菌 STPK 的生化和结构研究表明，细菌和真核 STPK 采用共同的折叠方式，并共享底物识别和调节的机制。分枝杆菌受体 STPK 通过两个不同的界面通过二聚化而被激活，这两个界面促进激活环磷酸化。活性 STPK 可在细菌细胞内磷酸化多种底物，包括其他激酶以及许多中心生理过程中涉及的蛋白质。就 FHA 结构域蛋白 GarA 而言，未磷酸化的蛋白调节初级代谢，而磷酸化介导 GarA 自身抑制。这些研究开始定义分枝杆菌 STPK 的激活机制和生物学调节功能。
