Abstract
Recent structural and biochemical investigations have come together to allow a better understanding of the mechanism of chaperonin (GroEL, Hsp60)–mediated protein folding, the final step in the accurate expression of genetic information. Major, asymmetric conformational changes in the GroEL double toroid accompany binding of ATP and the cochaperonin GroES. When a nonnative polypeptide, bound to one of the GroEL rings, is encapsulated by GroES to form a cis ternary complex, these changes drive the polypeptide into the sequestered cavity and initiate its folding. ATP hydrolysis in the cis ring primes release of the products, and ATP binding in the trans ring then disrupts the cis complex. This process allows the polypeptide to achieve its final native state, if folding was completed, or to recycle to another chaperonin molecule, if the folding process did not result in a form committed to the native state.
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Dates
Type | When |
---|---|
Created | 23 years ago (July 27, 2002, 7:42 a.m.) |
Deposited | 3 years, 10 months ago (Oct. 5, 2021, 9:50 a.m.) |
Indexed | 1 month, 2 weeks ago (July 11, 2025, 6:51 a.m.) |
Issued | 27 years, 2 months ago (June 1, 1998) |
Published | 27 years, 2 months ago (June 1, 1998) |
Published Print | 27 years, 2 months ago (June 1, 1998) |
@article{Sigler_1998, title={STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING}, volume={67}, ISSN={1545-4509}, url={http://dx.doi.org/10.1146/annurev.biochem.67.1.581}, DOI={10.1146/annurev.biochem.67.1.581}, number={1}, journal={Annual Review of Biochemistry}, publisher={Annual Reviews}, author={Sigler, Paul B. and Xu, Zhaohui and Rye, Hays S. and Burston, Steven G. and Fenton, Wayne A. and Horwich, Arthur L.}, year={1998}, month=jun, pages={581–608} }