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Article

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

The Journal of biological chemistry - 2 Sept 2011

Illingworth Melissa, Ramsey Andrew, Zheng Zhida, Chen Lingling

Abstract excerpt

In mediating protein folding, chaperonin GroEL and cochaperonin GroES form an enclosed chamber for substrate proteins in an ATP-dependent manner. The essential role of the double ring assembly of GroEL is demonstrated by the functional deficiency of the single ring GroEL(SR). The GroEL(SR)-GroES is highly stable with minimal ATPase activity. To restore the ATP cycle and the turnover of the folding chamber, we...

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Identifiers

PMID: 21757689
DOI: 10.1074/jbc.M111.255935
PMCID: PMC3162399

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Source receipt: pubmed, retrieved 7 Sept 2026.

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Research trail→

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Stimulating the substrate folding activity of a single ring GroEL variant by modulating the cochaperonin GroES.PMID 21757689Read ↗

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

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

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 ↗

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

From minichaperone to GroEL 2: importance of avidity of the multisite ring structure.Semantic proximity Read ↗

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