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The chaperonin folding machine |
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| Authors: | Saibil Helen R Ranson Neil A |
| Affiliation: | a School of Crystallography, Birkbeck College London, Malet Street, London, UK WC1E 7HX b School of Biochemistry and Molecular Biology, University of Leeds, Mount Preston Street, Leeds, UK LS2 9JT |
| Abstract: | Chaperonins are versatile molecular machines that assist the folding of a wide range of substrate proteins. They harness an ATPase cycle to control access of non-native proteins to hydrophobic binding sites. ATP binding promotes large conformational changes that partially bury the hydrophobic sites and initiate the binding of a co-chaperonin, creating closed and open cavities. Non-native proteins progress towards the native fold during their confinement in these cavities, and are then released by the allosteric action of ATP. |
| Keywords: | chaperone allostery molecular machine protein folding heat shock protein |
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