Putting a lid on protein folding: structure and function of the co-chaperonin, GroES. (Q41112868)

26 September 2017

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title

Putting a lid on protein folding: structure and function of the co-chaperonin, GroES. (English)

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26 September 2017

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Fenton WA

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26 September 2017

Weissman JS

series ordinal

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26 September 2017

Horwich AL

series ordinal

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26 September 2017

publication date

1 March 1996

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26 September 2017

published in

Chemistry and Biology

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26 September 2017

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26 September 2017

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26 September 2017

page(s)

157-161

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The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

26 September 2017

cites work

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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Residues in chaperonin GroEL required for polypeptide binding and release

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Protein folding in the cell

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Polypeptide interactions with molecular chaperones and their relationship to in vivo protein folding.

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Binding of chaperonins.

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Structure of holo-chaperonin studied with electron microscopy. Oligomeric cpn10 on top of two layers of cpn60 rings with two stripes each

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Symmetric complexes of GroE chaperonins as part of the functional cycle

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Biochemical Characterization of Symmetric GroEL-GroES Complexes

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The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures

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GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli.

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

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

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Cooperativity in ATP hydrolysis by GroEL is increased by GroES

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

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

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

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

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The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

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Chaperonin releases the substrate protein in a form with tendency to aggregate and ability to rebind to chaperonin

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

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Chaperonins can Catalyse the Reversal of Early Aggregation Steps when a Protein Misfolds

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7 January 2021

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

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7 January 2021

Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB

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7 January 2021

Characterization of a functionally important mobile domain of GroES.

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7 January 2021

10.1016/S1074-5521(96)90257-4

Identifiers

DOI

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26 September 2017

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