Abstract

The chaperonin GroEL and its cofactor GroES make up a molecular machine that rescues aggregation-prone misfolded proteins. The GroEL functional cycle consists of a series of large-scale allosteric transitions between the T, R, R′ and R″ states. The corresponding large structural rearrangements facilitate substrate protein capture, refolding, and release, and are thus essential for the proper operation of the chaperonin. Using a Cα-sidechain elastic network model-based structural perturbation method, that probes the response of a local perturbation at all residue sites, we have studied the molecular details of the T -> R and R″ ->T transitions and determined the key mechanical residues that support the allosteric cycle - the allostery wiring diagram. We provide a molecular level interpretation for the intraring positive cooperativity and interring negative cooperativity as well as the role of GroES in the GroEL allosteric cycle.

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