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Article

Probing the functional mechanism of Escherichia coli GroEL using circular permutation.

PloS one - 1 Jan 2011

Mizobata Tomohiro, Uemura Tatsuya, Isaji Kazuhiro, Hirayama Takuma, Hongo Kunihiro, Kawata Yasushi

Abstract excerpt

BACKGROUND: The Escherichia coli chaperonin GroEL subunit consists of three domains linked via two hinge regions, and each domain is responsible for a specific role in the functional mechanism. Here, we have used circular permutation to study the structural and functional characteristics of the GroEL subunit. METHODOLOGY/PRINCIPAL FINDINGS: Three soluble, partially active mutants with polypeptide ends relocated...

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Identifiers

PMID: 22028884
DOI: 10.1371/journal.pone.0026462
PMCID: PMC3196576

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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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