NDLI: A structural model for GroEL-polypeptide recognition.

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A structural model for GroEL-polypeptide recognition.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Fersht, A. R. Zahn, R. Buckle, A. M.
Description	Author Affiliation: Buckle AM ( Cambridge University Chemical Laboratory, Medical Research Council Centre, United Kingdom.);
Abstract	A monomeric peptide fragment of GroEL, consisting of residues 191-376, is a mini-chaperone with a functional chaperoning activity. We have solved the crystal structure at 1.7 A resolution of GroEL(191-376) with a 17-residue N-terminal tag. The N-terminal tag of one molecule binds in the active site of a neighboring molecule in the crystal. This appears to mimic the binding of a peptide substrate molecule. Seven substrate residues are bound in a relatively extended conformation. Interactions between the substrate and the active site are predominantly hydrophobic, but there are also four hydrogen bonds between the main chain of the substrate and side chains of the active site. Although the preferred conformation of a bound substrate is essentially extended, the flexibility of the active site may allow it to accommodate the binding of exposed hydrophobic surfaces in general, such as molten globule-type structures. GroEL can therefore help unfold proteins by binding to a hydrophobic region and exert a binding pressure toward the fully unfolded state, thus acting as an 'unfoldase.' The structure of the mini-chaperone is very similar to that of residues 191-376 in intact GroEL, so we can build it into GroEL and reconstruct how a peptide can bind to the tetradecamer. A ring of connected binding sites is noted that can explain many aspects of substrate binding and activity.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	8
Volume Number	94
Language	English
Publisher	National Academy of Sciences
Publisher Date	1997-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Chaperonin 60 Chemistry Models, Molecular Peptides Metabolism Escherichia Coli Protein Binding Protein Folding Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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