Conserved conformational changes in the ATPase cycle of human Hsp90. (Q46654083)

24 December 2017

title

Conserved conformational changes in the ATPase cycle of human Hsp90. (English)

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24 December 2017

Lukasz Skalniak

3

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Klaus Richter

object named as

Klaus Richter

1

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Johannes Buchner

object named as

Johannes Buchner

7

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author name string

Joanna Soroka

2

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24 December 2017

Adriane Leskovar

4

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24 December 2017

Martin Hessling

5

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24 December 2017

Jochen Reinstein

6

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24 December 2017

language of work or name

English

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publication date

9 April 2008

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24 December 2017

Journal of Biological Chemistry

published in

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24 December 2017

volume

283

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24 December 2017

page(s)

17757-17765

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24 December 2017

issue

26

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24 December 2017

Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery

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Pathways of chaperone-mediated protein folding in the cytosol

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ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo

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In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis

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Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements

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Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding

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Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex

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Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones

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The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains

21 January 2018

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Coordinated ATP hydrolysis by the Hsp90 dimer

21 January 2018

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N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle

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Intrinsic inhibition of the Hsp90 ATPase activity.

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Independent ATPase activity of Hsp90 subunits creates a flexible assembly platform

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Stimulation of the weak ATPase activity of human hsp90 by a client protein

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Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones

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Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1

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Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle

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The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle

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Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90

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Sti1 Is a Novel Activator of the Ssa Proteins

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The ATPase cycle of the endoplasmic chaperone Grp94.

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An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function

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Assessment of the ATP binding properties of Hsp90.

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The 43-kilodalton N-terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs.

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Monovalent cation dependence and preference of GHKL ATPases and kinases

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Dissection of the contribution of individual domains to the ATPase mechanism of Hsp90.

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GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway

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Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery.

21 January 2018

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The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo

21 January 2018

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Hsp90 isoforms: functions, expression and clinical importance

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Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone

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Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches.

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The ATPase cycle of the mitochondrial Hsp90 analog Trap1.

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21 January 2018

Identifiers

DOI

10.1074/JBC.M800540200

1 reference

24 December 2017

PubMed ID

18400751

1 reference

24 December 2017