Article
A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation.
Nature structural & molecular biology - 1 Nov 2004
Sewell B Trevor, Best Robert B, Chen Shaoxia, Roseman Alan M, Farr George W, Horwich Arthur L, Saibil Helen R
Abstract excerpt
The chaperonin GroEL assists protein folding through ATP-dependent, cooperative movements that alternately create folding chambers in its two rings. The substitution E461K at the interface between these two rings causes temperature-sensitive, defective protein folding in Escherichia coli. To understand the molecular defect, we have examined the mutant chaperonin by cryo-EM. The normal out-of-register alignment of...
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