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Article

Characterization of a functionally important mobile domain of GroES.

Nature - 15 Jul 1993

Landry S J, Zeilstra-Ryalls J, Fayet O, Georgopoulos C, Gierasch L M

Abstract excerpt

Although genetic and biochemical evidence has established that GroES is required for the full function of the molecular chaperone, GroEL, little is known about the molecular details of their interaction. GroES enhances the cooperativity of ATP binding and hydrolysis by GroEL (refs 4, 5) and is ne...

Topics

Amino Acid Sequence
Bacterial Proteins
Base Sequence
Chaperonin 10
Chaperonin 60
DNA, Bacterial
Escherichia coli
Heat-Shock Proteins
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Mutation
Peptide Fragments

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Binding

Protein Conformation

Source

Identifiers

PMID: 8100614
DOI: 10.1038/364255a0

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8100614-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Related research

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Click a neighbor to travelStep 1 · 12 closest

Characterization of a functionally important mobile domain of GroES.PMID 8100614Read ↗

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

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

Dissociation of the GroEL-GroES asymmetric complex is accelerated by increased cooperativity in ATP binding to the GroEL ring distal to GroES.Semantic proximity Read ↗

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

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

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

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

Compensatory changes in GroEL/Gp31 affinity as a mechanism for allele-specific genetic interaction.Semantic proximity Read ↗

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