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  C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycle

Weikl, T., Muschler, P., Richter, K., Veit, T., Reinstein, J., & Buchner, J. (2000). C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycle. Journal of Molecular Biology (London), 303, 583-592.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-2173-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-2177-0
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JMolBiol_303_2000_583.pdf (Any fulltext), 210KB
 
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 Creators:
Weikl, Tina, Author
Muschler, Paul, Author
Richter, Klaus, Author
Veit, Thomas, Author
Reinstein, Jochen1, Author              
Buchner, Johannes, Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: chaperone; MutL; MABA-ATP; kinetic analysis; mutagenesis
 Abstract: Hsp90 is an abundant molecular chaperone that functions in an ATP-dependent manner in vivo. The ATP-binding site is located in the N-terminal domain of Hsp90. Here, we dissect the ATPase cycle of Hsp90 kinetically. We find that Hsp90 binds ATP with a two-step mechanism. The rate-limiting step of the ATPase cycle is the hydrolysis of ATP. Importantly, ATP becomes trapped and committed to hydrolyze during the cycle. In the isolated ATP-binding domain of Hsp90, however, the bound ATP was not committed and the turnover numbers were markedly reduced. Analysis of a series of truncation mutants of Hsp90 showed that C-terminal regions far apart in sequence from the ATP-binding domain are essential for trapping the bound ATP and for maximum hydrolysis rates. Our results suggest that ATP binding and hydrolysis drive conformational changes that involve the entire molecule and lead to repositioning of the N and C-terminal domains of Hsp90.

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Language(s): eng - English
 Dates: 2000-09-042000-06-192000-09-042000-11-03
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Journal of Molecular Biology (London)
  Other : J Mol Biol
Source Genre: Journal
 Creator(s):
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Publ. Info: London : Academic Press, 4
Pages: - Volume / Issue: 303 Sequence Number: - Start / End Page: 583 - 592 Identifier: ISSN: 0022-2836
CoNE: https://pure.mpg.de/cone/journals/resource/954922646042