1OEL
CONFORMATIONAL VARIABILITY IN THE REFINED STRUCTURE OF THE CHAPERONIN GROEL AT 2.8 ANGSTROM RESOLUTION
Summary for 1OEL
Entry DOI | 10.2210/pdb1oel/pdb |
Descriptor | GROEL (HSP60 CLASS) (2 entities in total) |
Functional Keywords | chaperonin |
Biological source | Escherichia coli |
Cellular location | Cytoplasm: P0A6F5 |
Total number of polymer chains | 7 |
Total formula weight | 399898.05 |
Authors | Braig, K.,Adams, P.D.,Brunger, A.T. (deposition date: 1995-11-21, release date: 1996-04-03, Last modification date: 2024-02-14) |
Primary citation | Braig, K.,Adams, P.D.,Brunger, A.T. Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution. Nat.Struct.Biol., 2:1083-1094, 1995 Cited by PubMed 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. PubMed: 8846220DOI: 10.1038/nsb1295-1083 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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