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The ins and outs of a molecular chaperone machine
A Richardson1, S J Landry, C Georgopoulos
1Département de Biochimie Médicale, Université de Genève, Switzerland. Alexandra.Richardson@medicine.unige.ch
Trends in Biochemical Sciences
|May 19, 1998
Abstract:
Genetic and biochemical work has highlighted the biological importance of the GroEL/GroES (Hsp60/Hsp10; cpn60/cpn10) chaperone machine in protein folding. GroEL's donut-shaped structure has attracted the attention of structural biologists because of its elegance as well as the secrets (substrates) it can hide. The recent determination of the GroES and GroEL/GroES structures provides a glimpse of their plasticity, revealing dramatic conformational changes that point to an elaborate mechanism, coupling ATP hydrolysis to substrate release by GroEL.