The serine/threonine protein kinase E(PknE)in mycobacterium tuberculosis can inhibit apop-tosis of macrophages to allow the pathogens surviving in the host.PknE consists of an N-terminal intracel-lular kinase domain and a C-terminal extracellular sensor domain,which are joined by a single transmem-brane helix.In this experiment,the PknE extracellular sensor domain was cloned and expressed in the E.coli expression system.The protein crystallization conditions were screened after purification,and finally the crystal with a good shape was obtained.The diffraction data with the highest resolution of 0.175 nm was collected and processed in Shanghai Synchrotron Radiation Facility.All these experiments and data can lay the foundation for the structure determination of the PknE sensor domain which could be the useful infor-mation for structure-based drug discovery.
关键词
结核分枝杆菌/丝氨酸/苏氨酸蛋白激酶/PknE/表达纯化/结晶
Key words
mycobacterium tuberculosis/serine/threonine protein kinase/PknE/expression and purifica-tion/crystallization
维普
万方数据