1A6E

THERMOSOME-MG-ADP-ALF3 COMPLEX

Summary for 1A6E

• Entry DOI: 10.2210/pdb1a6e/pdb
• Descriptor: THERMOSOME (ALPHA SUBUNIT), THERMOSOME (BETA SUBUNIT), MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: thermoplasma acidophilum, group ii chaperonin, cct, tric, protein folding, atpase, transition state complex, atp hydrolysis, chaperonin
• Biological source: Thermoplasma acidophilum; More
• Total number of polymer chains: 2
• Total formula weight: 117947.41

Authors

Ditzel, L.,Loewe, J.,Stock, D.,Stetter, K.-O.,Huber, H.,Huber, R.,Steinbacher, S. (deposition date: 1998-02-24, release date: 1999-03-23, Last modification date: 2024-02-07)

Primary citation

Ditzel, L.,Lowe, J.,Stock, D.,Stetter, K.O.,Huber, H.,Huber, R.,Steinbacher, S.
Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT.
Cell(Cambridge,Mass.), 93:125-138, 1998

PubMed Abstract: 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.

PubMed: 9546398
DOI: 10.1016/S0092-8674(00)81152-6

Experimental method

X-RAY DIFFRACTION (3.2 Å)