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PubMed · 9519301

Structural aspects of GroEL function.

A Horovitz
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Abstract

The chaperonin GroEL and its cofactor GroES facilitate protein folding in an ATP-regulated manner. The recently solved crystal structure of the GroEL.GroES.(ADP)7 complex shows that the lining of the cavity in the polypeptide acceptor state is hydrophobic, whereas in the protein-release state it becomes hydrophilic. Other highlights of the past year include the visualization of the allosteric states of GroEL with respect to ATP using cryo-electron microscopy, and an X-ray crystallographic analysis of the interaction between the apical domain of GroEL and a peptide.

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Adenosine TriphosphateChaperonin 60CryopreservationCrystallography, X-RayMicroscopy, ElectronPeptidesProtein BindingProtein FoldingJournal ArticleResearch Support, Non-U.S. Gov'tReview

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A Horovitz. 1998. Structural aspects of GroEL function.. https://doi.org/10.1016/s0959-440x(98)80015-8

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