Structure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein 90

• 来源期刊: 生物化学与生物物理学报（英文版）
• 关键词: human Hsp90 N-terminal domain ATP hydrolysis catalytic mechanism
• 年，卷（期）: 2012,（4）
• 页码范围: 300-306
• 页数: 7页
• 语种: 英文
• DOI: 10.1093/abbs/gms001

摘要

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.