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Article

A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation.

Nature structural & molecular biology - 1 Nov 2004

Sewell B Trevor, Best Robert B, Chen Shaoxia, Roseman Alan M, Farr George W, Horwich Arthur L, Saibil Helen R

Abstract excerpt

The chaperonin GroEL assists protein folding through ATP-dependent, cooperative movements that alternately create folding chambers in its two rings. The substitution E461K at the interface between these two rings causes temperature-sensitive, defective protein folding in Escherichia coli. To unde...

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PMID: 15475965
DOI: 10.1038/nsmb844

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-15475965-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

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A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation.PMID 15475965Read ↗

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A dynamic model of long-range conformational adaptations triggered by nucleotide binding in GroEL-GroES.Semantic proximity Read ↗

Characterisation of a GroEL single-ring mutant that supports growth of Escherichia coli and has GroES-dependent ATPase activity.Semantic proximity Read ↗

Differential conformational modulations of MreB folding upon interactions with GroEL/ES and TRiC chaperonin components.Semantic proximity Read ↗

Stimulating the substrate folding activity of a single ring GroEL variant by modulating the cochaperonin GroES.Semantic proximity Read ↗

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Creating the Functional Single-Ring GroEL-GroES Chaperonin Systems via Modulating GroEL-GroES Interaction.Semantic proximity Read ↗

Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli.Semantic proximity Read ↗

Mapping pathways of allosteric communication in GroEL by analysis of correlated mutations.Semantic proximity Read ↗

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