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

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: 8846220
DOI: 10.1038/nsb1295-1083

Experimental method

X-RAY DIFFRACTION (2.8 Å)