1a6e
From Proteopedia
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| , resolution 3.2Å | |||||||
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| Sites: | and | ||||||
| Ligands: | , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THERMOSOME-MG-ADP-ALF3 COMPLEX
Overview
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.
About this Structure
1A6E is a Protein complex structure of sequences from Thermoplasma acidophilum. Full crystallographic information is available from OCA.
Reference
Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT., Ditzel L, Lowe J, Stock D, Stetter KO, Huber H, Huber R, Steinbacher S, Cell. 1998 Apr 3;93(1):125-38. PMID:9546398
Page seeded by OCA on Thu Mar 20 09:53:35 2008
Categories: Protein complex | Thermoplasma acidophilum | Ditzel, L. | Huber, H. | Huber, R. | Loewe, J. | Steinbacher, S. | Stetter, K O. | Stock, D. | ADP | AF3 | MG | Atp hydrolysis | Atpase | Cct | Group ii chaperonin | Protein folding | Transition state complex | Tric
