The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis (Q46113732)

19 December 2017

title

The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis (English)

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19 December 2017

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Moritz Mickler

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19 December 2017

Martin Hessling

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19 December 2017

Christoph Ratzke

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19 December 2017

Johannes Buchner

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19 December 2017

Thorsten Hugel

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19 December 2017

publication date

22 February 2009

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19 December 2017

Nature Structural & Molecular Biology

published in

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19 December 2017

volume

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19 December 2017

issue

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19 December 2017

page(s)

281-286

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19 December 2017

Structure and mechanism of the Hsp90 molecular chaperone machinery

cites work

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hsp90: twist and fold.

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A Grp on the Hsp90 mechanism

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

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

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Hsp90--from signal transduction to cell transformation.

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Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle

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Coordinated ATP hydrolysis by the Hsp90 dimer

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

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

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Single-molecule dynamics of mechanical coiled-coil unzipping.

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

31 March 2020

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Probing the interaction between two single molecules: fluorescence resonance energy transfer between a single donor and a single acceptor.

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Experimental test of connector rotation during DNA packaging into bacteriophage phi29 capsids

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Fueling protein DNA interactions inside porous nanocontainers.

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Myosin-V is a mechanical ratchet.

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Apo-Hsp90 coexists in two open conformational states in solution.

31 March 2020

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Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90.

31 March 2020

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Hsp90 structure: when two ends meet

31 March 2020

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The Hsp90 molecular chaperone: an open and shut case for treatment

31 March 2020

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Direct visualization of asymmetric adenine-nucleotide-induced conformational changes in MutL alpha

31 March 2020

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A practical guide to single-molecule FRET

31 March 2020

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The solution to multiple structures

31 March 2020

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Dimerization of Hsp90 is required for in vivo function. Design and analysis of monomers and dimers

31 March 2020

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A Reducing and Oxidizing System Minimizes Photobleaching and Blinking of Fluorescent Dyes

31 March 2020

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Measuring the rate of intramolecular contact formation in polypeptides

31 March 2020

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Folding at the speed limit

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31 March 2020

Identifiers

DOI

10.1038/NSMB.1557

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19 December 2017

Dimensions Publication ID

1040858834

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19 December 2017