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Curr Opin Struct Biol. 1998 Feb;8(1):93-100.

Structural aspects of GroEL function.

Author information

1
Department of Structural Biology, Weizmann Institute, Rehovot, Israel. csamnon@weizmann.weizmann.ac.il

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.

PMID:
9519301
[Indexed for MEDLINE]

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