1a6e | pdb_00001a6e

THERMOSOME-MG-ADP-ALF3 COMPLEX

spinqualitylabelsall models 1a6e, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1a6e is a 2 chain structure with sequence from Thermoplasma acidophilum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.2Å Ligands: ADP, AF3, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function THSA_THEAC Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chaperonin 3D structures

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