Elucidation of steps in the capture of a protein substrate for efficient encapsulation by GroE. (Q54465588)

30 May 2018

title

Elucidation of steps in the capture of a protein substrate for efficient encapsulation by GroE. (English)

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30 May 2018

author name string

Matthew J Cliff

1

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30 May 2018

Claire Limpkin

2

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30 May 2018

Angus Cameron

3

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30 May 2018

Steven G Burston

4

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30 May 2018

Anthony R Clarke

5

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30 May 2018

language of work or name

English

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publication date

9 May 2006

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30 May 2018

Journal of Biological Chemistry

published in

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30 May 2018

volume

281

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30 May 2018

issue

30

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30 May 2018

page(s)

21266-21275

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30 May 2018

Chaperonin-mediated protein folding

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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

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

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

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

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Binding of a chaperonin to the folding intermediates of lactate dehydrogenase

21 January 2018

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

21 January 2018

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Promotion of the in vitro renaturation of dodecameric glutamine synthetase from Escherichia coli in the presence of GroEL (chaperonin-60) and ATP.

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Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding.

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

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Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings

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Residues in chaperonin GroEL required for polypeptide binding and release

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

21 January 2018

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The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity

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

21 January 2018

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

21 January 2018

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Dynamics of the GroEL-protein complex: effects of nucleotides and folding mutants.

21 January 2018

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Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL.

21 January 2018

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An Algorithm for Least-Squares Estimation of Nonlinear Parameters

21 January 2018

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Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.

21 January 2018

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The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

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

21 January 2018

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Structure and function in GroEL-mediated protein folding

21 January 2018

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GroE facilitates refolding of citrate synthase by suppressing aggregation

21 January 2018

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

21 January 2018

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

21 January 2018

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Transient kinetic analysis of adenosine 5'-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL

21 January 2018

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

21 January 2018

1 reference

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21 January 2018

Identifiers

DOI

10.1074/JBC.M601605200

1 reference

30 May 2018

PubMed ID

16684774

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30 May 2018