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Article

GroEL Ring Separation and Exchange in the Chaperonin Reaction.

Cell - 25 Jan 2018

Yan Xiao, Shi Qiaoyun, Bracher Andreas, Miličić Goran, Singh Amit K, Hartl F Ulrich, Hayer-Hartl Manajit

Abstract excerpt

The bacterial chaperonin GroEL and its cofactor, GroES, form a nano-cage for a single molecule of substrate protein (SP) to fold in isolation. GroEL and GroES undergo an ATP-regulated interaction cycle to close and open the folding cage. GroEL consists of two heptameric rings stacked back to back. Here, we show that GroEL undergoes transient ring separation, resulting in ring exchange between complexes. Ring...

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Identifiers

PMID: 29336887
DOI: 10.1016/j.cell.2017.12.010

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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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GroEL Ring Separation and Exchange in the Chaperonin Reaction.PMID 29336887Read ↗

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Crystal structure of a GroEL-ADP complex in the relaxed allosteric state at 2.7 Å resolution.Semantic proximity Read ↗

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