doi: 10.1016/s0092-8674(00)80408-0.
Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin
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- PMID: 9346243
- DOI: 10.1016/s0092-8674(00)80408-0
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Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin
Cell.
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Abstract
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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