GroEL domain

Figure 6.12 (a) Schematic diagram of one subunit of GroEL. The polypeptide chain is folded info three domains. The equatorial domain (green) is the largest domain, comprising 10 a helices, and is built up from both the N-tetminal and the C-terminal regions. 

Semirigid domains with hinges (GroEL, Fj-ATPase) Disorder to order transition (Kinesin)... 

Smoot, A.L. Panda, M. Brazil, B.T. Buckle, A.M. Fersht, A.R. Horowitz, P.M. The binding of bis-ANS to the isolated GroEL apical domain fragment induces the formation of a folding intermediate with increased hydrophobic surface not observed in tetradecameric GroEL. Biochemistry 2001, 40, 4484-4492. 

Fig. 6. Mode of peptide binding to the GroEL apical domain. Residues 197-335 of the apical domain are shown as a ribbon diagram, with three binding peptides (black) overlaid. The hydrophobic binding residues identified by mutagenesis (Fenton et al., 1994) are shown in light-colored, space-filling format. Also shown are side chains of the binding peptides that interact with the apical domain.

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