Journal
ACTA BIOCHIMICA ET BIOPHYSICA SINICA
Volume 44, Issue 4, Pages 300-306Publisher
OXFORD UNIV PRESS
DOI: 10.1093/abbs/gms001
Keywords
human Hsp90; N-terminal domain; ATP hydrolysis; catalytic mechanism
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Funding
- National Program on Key Basic Research Project [2011CB911102]
- Shanghai Institute of Applied Physics, Chinese Academy of Sciences [O95501C061]
- Important National Science & Technology Specific Projects [2010ZX09401-401]
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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.
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