Role of the -phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics (Q27642245)

6

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Axel T. Brunger

object named as

Axel T Brunger

5

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author name string

Charu Chaudhry

1

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George W Farr

2

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Matthew J Todd

3

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Hays S Rye

4

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Paul B Sigler

ATP-bound states of GroEL captured by cryo-electron microscopy

8

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language of work or name

English

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publication date

1 October 2003

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published in

The EMBO Journal

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volume

22

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issue

19

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page(s)

4877-87

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cites work

1 reference

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Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT

20 March 2017

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The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex

20 March 2017

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The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants

20 March 2017

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X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-

20 March 2017

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Fluoride complexes of aluminium or beryllium act on G-proteins as reversibly bound analogues of the gamma phosphate of GTP

20 March 2017

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Use of TLS parameters to model anisotropic displacements in macromolecular refinement

20 March 2017

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20 March 2017

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Efficient anisotropic refinement of macromolecular structures using FFT

29 September 2017

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

20 March 2017

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Molecular chaperones in the cytosol: from nascent chain to folded protein

20 March 2017

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A dynamic model for the allosteric mechanism of GroEL

20 March 2017

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The structural basis of the myosin ATPase activity

20 March 2017

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Application of fluorescence resonance energy transfer to the GroEL-GroES chaperonin reaction

20 March 2017

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Chaperonin-mediated protein folding

29 September 2017

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Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

29 September 2017

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Cytoplasmic chaperonin containing TCP-1: structural and functional characterization

29 September 2017

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Protein folding in the central cavity of the GroEL-GroES chaperonin complex

29 September 2017

1 reference

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Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding

29 September 2017

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Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates

29 September 2017

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Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES.

29 September 2017

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A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL.

29 September 2017

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The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL.

2 June 2018

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A cytoplasmic chaperonin that catalyzes beta-actin folding

2 June 2018

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The allosteric transition of GroEL induced by metal fluoride-ADP complexes

2 June 2018

1 reference

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Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis

27 November 2018

1 reference

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Nucleotide binding to the chaperonin GroEL: non-cooperative binding of ATP analogs and ADP, and cooperative effect of ATP.

27 November 2018

1 reference

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The cell as a collection of protein machines: preparing the next generation of molecular biologists

27 November 2018

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Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL.

27 November 2018

1 reference

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Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction

27 November 2018

1 reference

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Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.

27 November 2018

1 reference

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The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

27 November 2018

1 reference

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Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL.

27 November 2018

1 reference

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Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis

27 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=204461

Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent

27 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=204461

GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings

27 November 2018

1 reference

12 December 2020

Processing of X-ray diffraction data collected in oscillation mode

1 reference

12 December 2020

Myosin active-site trapping with vanadate ion

1 reference

12 December 2020

GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms

1 reference

12 December 2020

Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction

1 reference

12 December 2020

Structure and function in GroEL-mediated protein folding

1 reference

12 December 2020

Identifiers

DOI

10.1093/EMBOJ/CDG477

1 reference

4886951

4886951

1 reference

1 reference

1 reference