Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution.
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.
Braig
K
K
Department of Genetics, Yale University, New Haven, Connecticut 06510, USA.
Adams
P D
PD
Brünger
A T
AT
D001426:Bacterial Proteins / Q000737:chemistry / Q000648:ultrastructure; D018834:Chaperonin 60 / Q000737:chemistry* / Q000648:ultrastructure*; D003461:Crystallography; D004926:Escherichia coli / Q000737:chemistry; D011487:Protein Conformation
D001426:Bacterial Proteins; D018834:Chaperonin 60