(Q54467011)

30 May 2018

title

Amide hydrogen exchange reveals conformational changes in hsp70 chaperones important for allosteric regulation. (English)

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30 May 2018

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1

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Matthias P. Mayer

series ordinal

4

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30 May 2018

Bernd Bukau

series ordinal

3

object named as

Bernd Bukau

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Christian Graf

2

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language of work or name

English

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publication date

13 April 2006

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Journal of Biological Chemistry

published in

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volume

281

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issue

24

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30 May 2018

page(s)

16493-16501

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30 May 2018

Hsp70 chaperones: cellular functions and molecular mechanism

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Structural analysis of substrate binding by the molecular chaperone DnaK

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Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis

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The hydroxyl of threonine 13 of the bovine 70-kDa heat shock cognate protein is essential for transducing the ATP-induced conformational change

21 January 2018

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The 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains

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A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE.

21 January 2018

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The second step of ATP binding to DnaK induces peptide release.

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Regulatory region C of the E. coli heat shock transcription factor, sigma32, constitutes a DnaK binding site and is conserved among eubacteria.

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Mapping temperature-induced conformational changes in the Escherichia coli heat shock transcription factor sigma 32 by amide hydrogen exchange.

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Analysis of subsecond protein dynamics by amide hydrogen exchange and mass spectrometry using a quenched-flow setup

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Allosteric regulation of Hsp70 chaperones by a proline switch

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21 January 2018

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Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones

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Mutations in the substrate binding domain of the Escherichia coli 70 kDa molecular chaperone, DnaK, which alter substrate affinity or interdomain coupling

21 January 2018

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21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M600847200

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30 May 2018

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30 May 2018