title: Reaction Cycle of Chaperonin GroEL via Symmetric "Football" Intermediate.
abstract: Chaperonin GroEL is an essential chaperone that assists in protein folding in the cell. Since one GroEL ring binds one GroES heptamer, the GroEL double ring permits the formation of two types of GroEL:GroES complexes: asymmetric 1:1 "bullet"-shaped and symmetric 1:2 "football"-shaped GroEL:GroES2 complexes. There have been continuing debates about the mechanism and which complex is critical to the chaperonin-assisted folding. In this review, I summarize the recent progress on the football complex.
authors.affiliation: Department of Biomolecular Engineering, Graduate School of Biosciences and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 226-8501, Japan. Electronic address: taguchi@bio.titech.ac.jp.
authors.forename: Hideki
authors.initials: H
authors.lastname: Taguchi
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D018835:Chaperonin 10 / Q000737:chemistry / Q000378:metabolism*; D018834:Chaperonin 60 / Q000737:chemistry / Q000378:metabolism*; D018833:Chaperonins / Q000737:chemistry / Q000378:metabolism*; D004926:Escherichia coli; D031541:Fluorescence Resonance Energy Transfer; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D013379:Substrate Specificity
chemical_list: D018835:Chaperonin 10; D018834:Chaperonin 60; D000255:Adenosine Triphosphate; D018833:Chaperonins
keywords: GroEL; Hsp60; chaperone; chaperonin; protein folding