Ditzel, Lars and Loewe, Jan and Stock, Daniela and Stetter, Karl-Otto and Huber, Harald and Huber, Robert and Steinbacher, Stefan (1998) Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. CELL, 93 (1). pp. 125-138. ISSN 0092-8674,
Full text not available from this repository.Abstract
We have determined to 2.6 Angstrom 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 (alpha beta)(4)(alpha beta)(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 MS-ADP-AIF(3) suggests that the closed conformation corresponds to the ATP form.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | T-COMPLEX POLYPEPTIDE-1; GROEL-GROES COMPLEXES; MOLECULAR CHAPERONE; CYTOPLASMIC CHAPERONIN; HEAT-SHOCK; THERMOPHILIC ARCHAEBACTERIUM; SULFOLOBUS-SOLFATARICUS; PROTEIN SUBSTRATE; BINDING DOMAINS; ATP HYDROLYSIS; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie (Archaeenzentrum) > Prof. Dr. Dina Grohmann |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 05 Sep 2023 10:36 |
| Last Modified: | 05 Sep 2023 10:36 |
| URI: | https://pred.uni-regensburg.de/id/eprint/49944 |
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