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Article

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

Journal of molecular biology - 12 Mar 2010

Kovács Eszter, Sun Zhe, Liu Han, Scott David J, Karsisiotis Andreas I, Clarke Anthony R, Burston Steven G, Lund Peter A

Abstract excerpt

Binding and folding of substrate proteins by the molecular chaperone GroEL alternates between its two seven-membered rings in an ATP-regulated manner. The association of ATP and GroES to a polypeptide-bound ring of GroEL encapsulates the folding proteins in the central cavity of that ring (cis ring) and allows it to fold in a protected environment where the risk of aggregation is reduced. ATP hydrolysis in the...

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Identifiers

PMID: 20006619
DOI: 10.1016/j.jmb.2009.11.074

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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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Characterisation of a GroEL single-ring mutant that supports growth of Escherichia coli and has GroES-dependent ATPase activity.PMID 20006619Read ↗

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

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

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

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

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

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

Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL.Semantic proximity Read ↗

Kinetic analysis of ATP-dependent inter-ring communication in GroEL.Semantic proximity Read ↗

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

Triggering protein folding within the GroEL-GroES complex.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 ↗

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

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