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Article

Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL.

Nature - 21 Aug 1997

Rye H S, Burston S G, Fenton W A, Beechem J M, Xu Z, Sigler P B, Horwich A L

Abstract excerpt

The chaperonin GroEL is a double-ring structure with a central cavity in each ring that provides an environment for the efficient folding of proteins when capped by the co-chaperone GroES in the presence of adenine nucleotides. Productive folding of the substrate rhodanese has been observed in cis ternary complexes, where GroES and polypeptide are bound to the same ring, formed with either ATP, ADP or...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 9285593
DOI: 10.1038/42047

Genes

PNP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

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Click a neighbor to travelStep 1 · 12 closest

Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL.PMID 9285593Read ↗

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

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

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

Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction.Semantic proximity Read ↗

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

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

Coupling between protein folding and allostery in the GroE chaperonin system.Semantic proximity Read ↗

Functional characterization of an archaeal GroEL/GroES chaperonin system: significance of substrate encapsulation.Semantic proximity Read ↗

Crystal structure of a GroEL-ADP complex in the relaxed allosteric state at 2.7 Å resolution.Semantic proximity Read ↗

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

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

Elucidation of steps in the capture of a protein substrate for efficient encapsulation by GroE.Semantic proximity Read ↗

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