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Chaperonins are molecular machines that undergo large-scale ATP-driven conformational changes that are crucial for their protein folding function. These changes are concerted in the case of the prokaryotic chaperonin GroEL and sequential in the case of the eukaryotic chaperonin CCT (1). Experimental data (2) and lattice model simulations (3) that explore the implications of these different allosteric mechanisms for the folding function of chaperonins will be described. A second issue to be explored is the mechanism by which ligand binding at one site triggers conformational changes that are propagated over a large distance as in the case of ATP binding to GroEL. The potential of correlated mutation analysis (4) to shed light on this problem will be discussed.
References 1. Horovitz, A. & Willison, K. R. (2005) Curr. Opin. Struct. Biol. 15, 646-651. 2. Kipnis, Y., Papo, N., Haran, G. & Horovitz, A. (2007) Proc. Natl. Acad. Sci. USA 104, 3119-3124. 3. Jacob, E., Horovitz, A. & Unger, R. (2007) Bioinformatics, in press. 4. Noivirt, O., Eisenstein, M. & Horovitz, A. (2005) Protein Eng. Des. Sel. 18, 247-253. |
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