1a6e
From Proteopedia
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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] with MG, ADP and AF3 as [ligands]. 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 Mon Oct 29 16:52:10 2007
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
