Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines (Q46764297)

25 December 2017

title

Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines (English)

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25 December 2017

author name string

Andreas Martin

series ordinal

1

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25 December 2017

Tania A Baker

series ordinal

2

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25 December 2017

Robert T Sauer

series ordinal

3

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25 December 2017

language of work or name

English

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publication date

1 October 2005

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25 December 2017

published in

Nature

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25 December 2017

volume

437

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25 December 2017

issue

7062

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25 December 2017

page(s)

1115-1120

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25 December 2017

https://scigraph.springernature.com/pub.10.1038/nature04031

exact match

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cites work

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Dynamics of substrate denaturation and translocation by the ClpXP degradation machine

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Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP.

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Effects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machine

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Overlapping recognition determinants within the ssrA degradation tag allow modulation of proteolysis.

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Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine.

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Nucleotide-dependent substrate handoff from the SspB adaptor to the AAA+ ClpXP protease.

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Asymmetric interactions of ATP with the AAA+ ClpX6 unfoldase: allosteric control of a protein machine.

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The dTTPase mechanism of T7 DNA helicase resembles the binding change mechanism of the F1-ATPase

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Escherichia coli transcription termination factor Rho binds and hydrolyzes ATP using a single class of three sites

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The structures of HsIU and the ATP-dependent protease HsIU-HsIV

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Direct evidence that a conserved arginine in RuvB AAA+ ATPase acts as an allosteric effector for the ATPase activity of the adjacent subunit in a hexamer.

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A specificity-enhancing factor for the ClpXP degradation machine

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Partitioning between unfolding and release of native domains during ClpXP degradation determines substrate selectivity and partial processing

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ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal

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Regulation of the transcriptional activator NtrC1: structural studies of the regulatory and AAA+ ATPase domains

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The crystal structure of the bifunctional primase-helicase of bacteriophage T7

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Interactions between two catalytically distinct MCM subgroups are essential for coordinated ATP hydrolysis and DNA replication

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Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP

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7 January 2021

Sequential hydrolysis of ATP molecules bound in interacting catalytic sites of Escherichia coli transcription termination protein Rho

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7 January 2021

The N-terminal zinc binding domain of ClpX is a dimerization domain that modulates the chaperone function

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7 January 2021

Structure of the Rho transcription terminator: mechanism of mRNA recognition and helicase loading

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7 January 2021

Identifiers

DOI

10.1038/NATURE04031

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25 December 2017

Dimensions Publication ID

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25 December 2017