,Structure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein

• 作 者: Jian Li Lihua Sun Chunyan Xu Feng Yu Huan Zhou Yanlong Zhao Jian Zhang Jianhua Cai Cheney Mao Lin Tang Yechun Xu Jianhua He
• 机 构: Shanghai Institute of Applied Physics, Chinese Academy of Sciences, Shanghai 201204, China“,”Shangha
• 出 处: 生物化学与生物物理学报（英文版）
• 发表日期: 2012年4期
• 关键词: human Hsp90 N-terminal domain ATP hydrolysis catalytic mechanism

The activation of molecular chaperone heat-shock protein 90 (Hsp90) is dependent on ATP binding and hydrolysis,which occurs in the N-terminal domains of protein.Here,we have determined three crystal structures of the N-terminal domain of human Hsp90 in native and in complex with ATP and ATP analog,providing a clear view of the catalytic mechanism of ATP hydrolysis by Hsp90.Additionally,the binding of ATP leads the N-terminal domains to be an intermediate state that could be used to partially explain why the isolated N-terminal domain of Hsp90 has very weak ATP hydrolytic activity.