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Article

Crystal structure of a symmetric football-shaped GroEL:GroES2-ATP14 complex determined at 3.8Å reveals rearrangement between two GroEL rings.

Journal of molecular biology - 23 Oct 2014

Koike-Takeshita Ayumi, Arakawa Takatoshi, Taguchi Hideki, Shimamura Tatsuro

Abstract excerpt

The chaperonin GroEL is an essential chaperone that assists in protein folding with the aid of GroES and ATP. GroEL forms a double-ring structure, and both rings can bind GroES in the presence of ATP. Recent progress on the GroEL mechanism has revealed the importance of a symmetric 1:2 GroEL:GroES2 complex (the "football"-shaped complex) as a critical intermediate during the functional GroEL cycle. We determined...

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Identifiers

PMID: 25174333
DOI: 10.1016/j.jmb.2014.08.017

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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 a symmetric football-shaped GroEL:GroES2-ATP14 complex determined at 3.8Å reveals rearrangement between two GroEL rings.PMID 25174333Read ↗

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