A monomeric variant of GroEL binds nucleotides but is inactive as a molecular chaperone.

doi:10.1074/jbc.270.35.20404

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Article

A monomeric variant of GroEL binds nucleotides but is inactive as a molecular chaperone.

The Journal of biological chemistry - 1 Sept 1995

White Z W, Fisher K E, Eisenstein E

Abstract excerpt

The heat shock protein GroEL from Escherichia coli is a tetradecameric oligomer that facilitates the refolding of nonnative polypeptides in an ATP-hydrolysis dependent reaction. A mutant in GroEL was prepared in which lysine 3 was substituted with glutamate, which destabilizes the oligomeric structure of GroEL (Horovitz, A., Bochkareva, E.S., and Girshovich, A.S. (1993) J. Biol. Chem. 268, 9957-9959). The highly...

Topics

Adenosine Diphosphate
Adenosine Triphosphate
Anilino Naphthalenesulfonates
Binding Sites
Chaperonin 60
Chaperonins
Circular Dichroism
Cloning, Molecular
Escherichia coli
Fluorescent Dyes
Genetic Variation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Kinetics

Molecular Weight

Mutagenesis, Site-Directed

Phosphopyruvate Hydratase

Protein Binding

Protein Conformation

Protein Denaturation

Source

Open in PubMed

Identifiers

PMID: 7657615
DOI: 10.1074/jbc.270.35.20404

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7657615-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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