Structural basis of allosteric changes in the GroEL mutant Arg197--&gt;Ala (Q73711185)

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6 November 2019

title

Structural basis of allosteric changes in the GroEL mutant Arg197-->Ala (English)

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6 November 2019

author name string

H E White

1

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6 November 2019

S Chen

2

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6 November 2019

A M Roseman

3

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6 November 2019

O Yifrach

4

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6 November 2019

A Horovitz

5

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6 November 2019

H R Saibil

6

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6 November 2019

publication date

1 September 1997

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Nature structural biology

6 November 2019

published in

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6 November 2019

volume

4

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6 November 2019

issue

9

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6 November 2019

page(s)

690-694

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

6 November 2019

cites work

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

Residues in chaperonin GroEL required for polypeptide binding and release

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196-->Ala.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

Allosteric control by ATP of non-folded protein binding to GroEL

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

Cooperativity in ATP hydrolysis by GroEL is increased by GroES

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

Detection of changes in pairwise interactions during allosteric transitions: coupling between local and global conformational changes in GroEL

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

Chaperone activity and structure of monomeric polypeptide binding domains of GroEL

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

A structural model for GroEL-polypeptide recognition

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

Strength and co-operativity of contributions of surface salt bridges to protein stability

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

Escherichia coli aspartate transcarbamoylase: the molecular basis for a concerted allosteric transition

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

Mechanisms of cooperativity and allosteric regulation in proteins

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB0997-690

31 March 2020

Identifiers

DOI

10.1038/NSB0997-690

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9302993%20AND%20SRC:MED&resulttype=core&format=json

6 November 2019

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