1EGS
NMR STRUCTURE OF GROES MOBILE LOOP RESIDUES 19-27 IN THE SYNTHETIC PEPTIDE (RESIDUES 13-32) BOUND TO GROEL, 20 STRUCTURES
Summary for 1EGS
| Entry DOI | 10.2210/pdb1egs/pdb |
| Descriptor | GROES (1 entity in total) |
| Functional Keywords | chaperonin, protein folding, heat shock |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 870.05 |
| Authors | Landry, S.J. (deposition date: 1997-06-30, release date: 1997-09-17, Last modification date: 2024-10-23) |
| Primary citation | Landry, S.J.,Taher, A.,Georgopoulos, C.,van der Vies, S.M. Interplay of structure and disorder in cochaperonin mobile loops. Proc.Natl.Acad.Sci.USA, 93:11622-11627, 1996 Cited by PubMed Abstract: Protein-protein interactions typically are characterized by highly specific interfaces that mediate binding with precisely tuned affinities. Binding of the Escherichia coli cochaperonin GroES to chaperonin GroEL is mediated, at least in part, by a mobile polypeptide loop in GroES that becomes immobilized in the GroEL/GroES/nucleotide complex. The bacteriophage T4 cochaperonin Gp31 possesses a similar highly flexible polypeptide loop in a region of the protein that shows low, but significant, amino acid similarity with GroES and other cochaperonins. When bound to GroEL, a synthetic peptide representing the mobile loop of either GroES or Gp31 adopts a characteristic bulged hairpin conformation as determined by transferred nuclear Overhauser effects in NMR spectra. Thermodynamic considerations suggest that flexible disorder in the cochaperonin mobile loops moderates their affinity for GroEL to facilitate cycles of chaperonin-mediated protein folding. PubMed: 8876186DOI: 10.1073/pnas.93.21.11622 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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