The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S (Q70907195)

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14 October 2019

title

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

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14 October 2019

3

Otwinowski Z

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14 October 2019

author name string

Boisvert DC

1

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14 October 2019

Wang J

2

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14 October 2019

Horwich AL

4

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14 October 2019

Sigler PB

5

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14 October 2019

publication date

1 February 1996

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Nature structural biology

14 October 2019

published in

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14 October 2019

volume

3

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14 October 2019

page(s)

170-177

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14 October 2019

issue

2

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Purification and properties of groE, a host protein involved in bacteriophage assembly

14 October 2019

cites work

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Homologous plant and bacterial proteins chaperone oligomeric protein assembly

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A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene

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A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1.

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A cytoplasmic chaperonin that catalyzes beta-actin folding

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Molecular chaperone functions of heat-shock proteins

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Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1

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The chaperonin cycle and protein folding

31 March 2020

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

31 March 2020

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31 March 2020

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Protein folding in the cell

31 March 2020

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Molecular chaperones in cellular protein folding

31 March 2020

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The chaperonin GroEL binds a polypeptide in an .alpha.-helical conformation

31 March 2020

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Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. I. GroEL recognizes the signal sequences of beta-lactamase precursor.

31 March 2020

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The hydrophobic nature of GroEL-substrate binding

31 March 2020

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ATP induces large quaternary rearrangements in a cage-like chaperonin structure.

31 March 2020

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A polypeptide bound by the chaperonin groEL is localized within a central cavity

31 March 2020

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Folding intermediate binds to the bottom of bullet-shaped holo-chaperonin and is readily accessible to antibody.

31 March 2020

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Residues in chaperonin GroEL required for polypeptide binding and release

31 March 2020

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

31 March 2020

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The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.

31 March 2020

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

31 March 2020

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Improved Fourier coefficients for maps using phases from partial structures with errors

31 March 2020

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Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains.

31 March 2020

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Increased efficiency of GroE-assisted protein folding by manganese ions

31 March 2020

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

31 March 2020

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

31 March 2020

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The effect of carboxyl-terminal mutagenesis of Gt alpha on rhodopsin and guanine nucleotide binding

31 March 2020

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

31 March 2020

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Mutation Ala2-->Ser destabilizes intersubunit interactions in the molecular chaperone GroEL.

31 March 2020

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Improved methods for building protein models in electron density maps and the location of errors in these models

31 March 2020

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Assessment of protein models with three-dimensional profiles

31 March 2020

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

31 March 2020

1 reference

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PROCHECK: a program to check the stereochemical quality of protein structures

31 March 2020

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Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES.

31 March 2020

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31 March 2020

Identifiers

DOI

10.1038/NSB0296-170

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8564544%20AND%20SRC:MED&resulttype=core&format=json

14 October 2019

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