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Article

Crystal structure of the temperature-sensitive and allosteric-defective chaperonin GroELE461K.

Journal of structural biology - 1 Sept 2006

Cabo-Bilbao Aintzane, Spinelli Silvia, Sot Begoña, Agirre Jon, Mechaly Ariel E, Muga Arturo, Guérin Diego M A

Abstract excerpt

The chaperonin GroEL adopts a double-ring structure with various modes of allosteric communication. The simultaneous positive intra-ring and negative inter-ring co-operativities alternate the functionality of the folding cavities in both protein rings. Negative inter-ring co-operativity is maintained through different inter-ring interactions, including a salt bridge involving Glu 461. Replacement of this residue...

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Identifiers

PMID: 16904907
DOI: 10.1016/j.jsb.2006.06.008

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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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Crystal structure of the temperature-sensitive and allosteric-defective chaperonin GroELE461K.PMID 16904907Read ↗

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