Reference: Ditzel L, et al. (1998) Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell 93(1):125-38

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Abstract


We have determined to 2.6 A resolution the crystal structure of the thermosome, the archaeal group II chaperonin from T. acidophilum. The hexadecameric homolog of the eukaryotic chaperonin CCT/TRiC shows an (alphabeta)4(alphabeta)4 subunit assembly. Domain folds are homologous to GroEL but form a novel type of inter-ring contact. The domain arrangement resembles the GroEL-GroES cis-ring. Parts of the apical domains form a lid creating a closed conformation. The lid substitutes for a GroES-like cochaperonin that is absent in the CCT/TRiC system. The central cavity has a polar surface implicated in protein folding. Binding of the transition state analog Mg-ADP-AIF3 suggests that the closed conformation corresponds to the ATP form.

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Journal Article | Research Support, Non-U.S. Gov't
Authors
Ditzel L, Löwe J, Stock D, Stetter KO, Huber H, Huber R, Steinbacher S
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