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Cell. 1997 Oct 17;91(2):263-70.

Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin.

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Department of Molecular Structural Biology, Max-Planck-Institute for Biochemistry, Planegg-Martinsried, Germany.


The crystal structure of the substrate binding domain of the thermosome, the archaeal group II chaperonin, has been determined at 2.3 A resolution. The core resembles the apical domain of GroEL but lacks the hydrophobic residues implied in binding of substrates to group I chaperonins. Rather, a large hydrophobic surface patch is found in a novel helix-turn-helix motif, which is characteristic of all group II chaperonins including the eukaryotic TRiC/CCT complex. Models of the holochaperonin, which are consistent with cryo electron microscopy data, suggest a dual role of this helical protrusion in substrate binding and controlling access to the central cavity independent of a GroES-like cochaperonin.

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