1oel
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CONFORMATIONAL VARIABILITY IN THE REFINED STRUCTURE OF THE CHAPERONIN GROEL AT 2.8 ANGSTROM RESOLUTION
OverviewOverview
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 StructureAbout this Structure
1OEL is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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
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