EC Number   |
Reference |
|---|
   5.6.1.7 | - |
701251 |
| 5.6.1.7 | 2-dimensional crystals of the beta subunits of the chaperonin TF55 from Sulfolobus shibatae reconstituted into oligomers in the absence of alpha subunits. The subunits form rings with 9-fold rotational symmetry which arrange themselves in a trigonal lattice |
678371 |
| 5.6.1.7 | AMP-PNP-bound enzyme form, vapor batch crystallization method, using 20 mM MgCl2, 100 mM HEPES-NaOH (pH 7.5), and 22% (w/v) polyacrylic acid 5100. ADP-bound enzyme form, vapor batch crystallization method, using 200 mM NH4Cl, 10 mM MgCl2, 50 mM HEPES sodium (pH 7.0), 5% (w/v) polyethylene glycol PEG 8000, and 3% (w/v) 1,8-diaminooctane |
751294 |
| 5.6.1.7 | analysis of crystal structures of the GroE chaperonin from Escherichia coli in the open, ATP-bound, PDB ID 1KP8, and closed, PDB ID 1AON, states |
735006 |
| 5.6.1.7 | analysis of the X-ray crystal structures of GroEL and GroEL-GroES complexes in absence or presence of ATP, PDB IDs 1OEL and 1SVT, and of enzyme mutant E461K interface, PDB ID 2EU1 |
734473 |
| 5.6.1.7 | atomic force microscope imaging of enzyme without any preparation technique. Evidence for the presence of two distinct structures of the complex, which probably correspond to the open and closed conformations. Enzyme exists in solution as both single-ring and double-ring complexes |
677908 |
| 5.6.1.7 | crystal structure of the native GroEL-GroES-ADP homolog with substrate proteins in the cis-cavity, at 2.8 A resolution. Twenty-four in vivo substrate proteins within the cis-cavity are identified from the crystals |
670902 |
| 5.6.1.7 | crystals of GroELE461K are grown at 4°C in hanging-drop vapour-diffusion experiments. The crystal structure of the mutant chaperonin GroELE461K is determined at 3.3 A and compared with other structures |
670046 |
| 5.6.1.7 | electron cryo-microscopy study. Enzyme shows symmetric open and closed forms and an asymmetric form resembling a flattened GroEL-GroES bullet complex. The closed rings of the Sulfolobus chaperonin correspond to nucleotide-bound, and the open rings to nucleotide-free forms |
681371 |
| 5.6.1.7 | electron microscopy and circular dichroism study reveal two distinct conformational states that are part of chaperonin functional cycle. The closed archaeosome complex binds ATP and forms an open complex. Upon ATP hydrolysis, the open complex dissociates into subunits. Free subunits reassemble into a two-ring structure |
680597 |
