Chaperonin GroEL: Structure and Reaction Cycle

Title: Chaperonin GroEL: Structure and Reaction Cycle

Volume: 8 Issue: 5

Author(s): K. Ananda Krishna, G. Venkateswara Rao and K. R.S. Sambasiva Rao

Affiliation:

Keywords: Chaperonin, Escherichia coli, iterative annealing, molecular chaperonins, GroEL, GroES, protein folding

Abstract: The structure of Escherichia coli chaperonin GroEL was studied using various experimental tools. Such studies produced information about its structure with increasing details. Moreover, remarkable advances in experimental methods provided a step forward in understanding the reaction cycle involved in GroEL-mediated protein folding. In the current review we summarize recent progress, focus on the structure of GroEL and understand the mechanism involved in GroEL-mediated protein folding. This review is divided into the following sections: (i) Section 1 provides basic understanding on protein folding, (ii) Section 2 not only describes various tools used to elucidate the structural aspects of GroEL but also provides details about its structure with particular emphasis, (iii) Section 3 describes allosteric transitions and the reaction cycle involved in GroEL-mediated protein folding, (iv) Section 4 explains iterative annealing and smoothing of the energy landscape model and finally (v) Section 5 discusses applications and recent progress.

Cite this article as:

Krishna Ananda K., Rao Venkateswara G. and Rao R.S. Sambasiva K., Chaperonin GroEL: Structure and Reaction Cycle, Current Protein & Peptide Science 2007; 8 (5) . https://dx.doi.org/10.2174/138920307782411455