Chaperonin GroEL: structure and reaction cycle.
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.
Krishna
K Ananda
KA
Center for Biotechnology, Acharya Nagarjuna University, Guntur 522 510, Andhra Pradesh, India.
Rao
G Venkateswara
GV
Rao
K R S Sambasiva
KR
D000494:Allosteric Regulation; D018834:Chaperonin 60 / Q000737:chemistry* / Q000378:metabolism; D018833:Chaperonins / Q000737:chemistry / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism; D008956:Models, Chemical; D008958:Models, Molecular; D017510:Protein Folding
D018834:Chaperonin 60; D029968:Escherichia coli Proteins; D018833:Chaperonins