GroEL, Chaperonin

Figure 6.11 Schematic diagram of the chaperonin GroEL molecule as a cylinder with 14 subunits arranged in two tings of 7 subunits each. The space occupied by one subunit is red and the hole inside the cylinder is blue.

Fenton, W.A., et al. Residues in chaperonin GroEL required for polypeptide binding and release. 

Enzymes assist formation of proper disulfide bonds during folding Isomerization of proline residues can be a rate-limiting step in protein folding Proteins can fold or unfold inside chaperonins GroEL is a cylindrical structure with a... 

Yu, M., Goldberg, S., Goldberg, A.L. (1W2). Heat shock in Escherichia coli alters the protein-binding properties of the chaperonin groEL by inducing its phosphorylation. Nature 357, 167-169. 

Houry, W. A., Frishman, D., Eckerskom, C., Lottspeich, F., and Hartl, F. U. (1999). Identification of in vivo substrates ofthe chaperonin GroEL. Nature 402, 147-154. 

K. Braig, P. Adams, and A.T. Brunger, Conformational Variability in the Refined Structure of the Chaperonin GroEL at 2.8 A Resolution. Nature Struct. Biol, 2,1083-1094,1995. 

O. Yifrach and A. Horovitz, Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL. Biochemistry 34, 5303-5308 (1995). 

W. A. Fenton, Y. Kashi, K. Furtak, and A. L. Horwich, Residues in chaperonin GroEL required for polypeptide binding and release. Nature 371, 614-619 (1994). 

Peralta D, Hartman DJ, Hoogenraad NJ and Hoj PB. Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES. FEBS Lett. 1994 339 45-49. 

E.A. Bramhall, R.L. Cross, S. Rospert, N.K. Steede, S.J. Landry, Identification of amino acid residues at nucleotide-binding sites of chaperonin GroEL/GroES and cpnlO by photoafBnity labeling with 2-azido-adenosine 5 -triphosphate, Eur. J. Biochem., 1997, 244, 627-634. 

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