1egs

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NMR STRUCTURE OF GROES MOBILE LOOP RESIDUES 19-27 IN THE SYNTHETIC PEPTIDE (RESIDUES 13-32) BOUND TO GROEL, 20 STRUCTURES

Overview

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.

About this Structure

1EGS is a Single protein structure of sequence from Escherichia coli with ACE and NH2 as ligands. Full crystallographic information is available from OCA.

Reference

Interplay of structure and disorder in cochaperonin mobile loops., Landry SJ, Taher A, Georgopoulos C, van der Vies SM, Proc Natl Acad Sci U S A. 1996 Oct 15;93(21):11622-7. PMID:8876186

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