| Автор | Sigler, Paul B. |
| Автор | Xu, Zhaohui |
| Автор | Rye, Hays S. |
| Автор | Burston, Steven G. |
| Автор | Fenton, Wayne A. |
| Автор | Horwich, Arthur L. |
| Дата выпуска | 1998 |
| dc.description | ▪ 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. |
| Формат | application.pdf |
| Издатель | Annual Reviews |
| Копирайт | Annual Reviews |
| Название | STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING |
| DOI | 10.1146/annurev.biochem.67.1.581 |
| Print ISSN | 0066-4154 |
| Журнал | Annual Review of Biochemistry |
| Том | 67 |
| Первая страница | 581 |
| Последняя страница | 608 |
| Аффилиация | Sigler, Paul B.; Department of Molecular Biophysics and Biochemistry, 3Department of Genetics, School of Medicine, 2Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06510; e-mail: sigler@csb.yale.edu |
