1oel
From Proteopedia
CONFORMATIONAL VARIABILITY IN THE REFINED STRUCTURE OF THE CHAPERONIN GROEL AT 2.8 ANGSTROM RESOLUTION
Overview
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.
About this Structure
1OEL is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution., Braig K, Adams PD, Brunger AT, Nat Struct Biol. 1995 Dec;2(12):1083-94. PMID:8846220 Page seeded by OCA on Sat May 3 03:44:58 2008
