Research Article
Mapping pathways of allosteric communication in GroEL by analysis of correlated mutations
Article first published online: 12 JUL 2002
DOI: 10.1002/prot.10180
Copyright © 2002 Wiley-Liss, Inc.
Issue
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Proteins: Structure, Function, and Bioinformatics
Volume 48, Issue 4, pages 611–617, 1 September 2002
Additional Information
How to Cite
Kass, I. and Horovitz, A. (2002), Mapping pathways of allosteric communication in GroEL by analysis of correlated mutations. Proteins: Structure, Function, and Bioinformatics, 48: 611–617. doi: 10.1002/prot.10180
Publication History
- Issue published online: 12 JUL 2002
- Article first published online: 12 JUL 2002
- Manuscript Accepted: 18 APR 2002
- Manuscript Received: 8 FEB 2002
Funded by
- Israel Science Foundation administered by The Israel Academy of Sciences and Humanities
- MINERVA Foundation, Germany
- Abstract
- Article
- References
- Cited By
Keywords:
- nested allostery;
- cooperativity;
- GroES;
- chaperonins;
- molecular chaperones;
- protein folding
Abstract
An interesting example of an allosteric protein is the chaperonin GroEL. It undergoes adenosine 5′-triphosphate-induced conformational changes that are reflected in binding of adenosine 5′-triphosphate with positive cooperativity within rings and negative cooperativity between rings. Herein, correlated mutations in chaperonins are analyzed to unravel routes of allosteric communication in GroEL and in its complex with its co-chaperonin GroES. It is shown that analysis of correlated mutations in the chaperonin family can provide information about pathways of allosteric communication within GroEL and between GroEL and GroES. The results are discussed in the context of available structural, genetic, and biochemical data concerning short- and long-range interactions in the GroE system. Proteins 2002;48:611–617. © 2002 Wiley-Liss, Inc.

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