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Article

Isolation and characterisation of mutants of GroEL that are fully functional as single rings.

Journal of molecular biology - 19 Sept 2003

Sun Zhe, Scott David J, Lund Peter A

Abstract excerpt

A key aspect of the reaction mechanism for the molecular chaperone GroEL is the transmission of an allosteric signal between the two rings of the GroEL complex. Thus, the single-ring mutant SR1 is unable to act as a chaperone as it cannot release bound substrate or GroES. We used a simple selection procedure to identify mutants of SR1 that restored chaperone activity in vivo. A large number of single amino acid...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 12963378
DOI: 10.1016/s0022-2836(03)00830-1

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Isolation and characterisation of mutants of GroEL that are fully functional as single rings.PMID 12963378Read ↗

Characterisation of mutations in GroES that allow GroEL to function as a single ring.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 ↗

From minichaperone to GroEL 3: properties of an active single-ring mutant of GroEL.Semantic proximity Read ↗

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

A kinetic analysis of the nucleotide-induced allosteric transitions in a single-ring mutant of GroEL.Semantic proximity Read ↗

Effective ATPase activity and moderate chaperonin-cochaperonin interaction are important for the functional single-ring chaperonin system.Semantic proximity Read ↗

In vivo and in vitro function of GroEL mutants with impaired allosteric properties.Semantic proximity Read ↗

GroEL Ring Separation and Exchange in the Chaperonin Reaction.Semantic proximity Read ↗

Triggering protein folding within the GroEL-GroES complex.Semantic proximity Read ↗

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

Crystal structure of a symmetric football-shaped GroEL:GroES2-ATP14 complex determined at 3.8Å reveals rearrangement between two GroEL rings.Semantic proximity Read ↗

Functional communications between the apical and equatorial domains of GroEL through the intermediate domain.Semantic proximity Read ↗

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