摘要
大鼠脑驱动蛋白(rat brain kinesin)是一种利用水解ATP所释放的能量,在微管束上高速且连续性运动的常规驱动蛋白.它在神经突触的物质运输中起着重要作用.研究大鼠脑驱动蛋白是如何将ATP中储藏的化学能转化为机械动能,是理解其运动机能的重要课题.本课题获得了大鼠脑驱动蛋白单体与ATP结构类似物AMPPCP形成的复合物晶体结构.将这个晶体结构与大鼠脑驱动蛋白单体-另一种ATP结构类似物AMPPNP形成的复合物晶体结构以及大鼠脑驱动蛋白单体-ATP水解产物ADP形成的复合物晶体结构进行相互比较,揭示了其活性中心的开关区域I中丝氨酸203可能作为质子的供体,加速了ATP中γ-磷酸和β-磷酸的断裂,从而导致ATP的水解.
Rat brain kinesin is a conventional kinesin that uses the chemical energy from ATP hydrolysis to walk along the microtubule filaments with high speed and process. Studies on how the chemical energy in ATP is transformed to mechanical movement are vital to understand its moving function. Analysis of the crystal structure of monomeric rat brain kinesin complexed with an ATP analog,AMPPCP,and its comparison with the complex structures with another ATP analog,AMPPNP,and its ATP hydrolyzed product,ADP,reveal the important role of Ser203 in the Switch I region. This key residue may act as a proton donor to promote the linkage break between γ-phoshate and β-phosphate in the initial step of ATP hydrolysis.
出处
《中国生物化学与分子生物学报》
CAS
CSCD
北大核心
2015年第1期96-102,共7页
Chinese Journal of Biochemistry and Molecular Biology
基金
扬州大学科技培育基金(No.2013CXJ083)
教育部留学回国人员科研启动基金资助~~
