PMID:8846220
| Citation |
Braig, K, Adams, PD and Brünger, AT (1995) Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution. Nat. Struct. Biol. 2:1083-94 |
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| Abstract |
Improved refinement of the crystal structure of GroEL from Escherichia coli has resulted in a complete atomic model for the first 524 residues. A new torsion-angle dynamics method and non-crystallographic symmetry restraints were used in the refinement. The model indicates that conformational variability exists due to rigid-body movements between the apical and intermediate domains of GroEL, resulting in deviations from strict seven-fold symmetry. The regions of the protein involved in polypeptide and GroES binding show unusually high B factors; these values may indicate mobility or discrete disorder. The variability of these regions may play a role in the ability of GroEL to bind a wide variety of substrates. |
| Links | |
| Keywords |
Bacterial Proteins/chemistry; Bacterial Proteins/ultrastructure; Chaperonin 60/chemistry; Chaperonin 60/ultrastructure; Crystallography; Escherichia coli/chemistry; Protein Conformation |
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