Prediction of the structure of GroES and its interaction with GroEL.
The three-dimensional structure of the GroES monomer and its interaction with GroEL has been predicted using a combination of prediction tools and experimental data obtained by biophysical [electron microscope (EM), Fourier transform infrared (FTIR), and nuclear magnetic resonance (NMR)] and biochemical techniques. The GroES monomer, according to the prediction, is composed of eight beta-strands forming a beta-barrel with loose ends. In the model, beta-strands 5-8 run along the outer surface of GroES, forming an antiparallel beta-sheet with beta 4 loosely bound to one of the edges. beta-strands 1-3 would then be parallel and placed in the interior of the molecule. Loops 1-3 would face the internal cavity of the GroEL-GroES complex, and together with conserved residues in loops 5 and 7, would form the active surface interacting with GroEL.
D000595:Amino Acid Sequence; D001665:Binding Sites; D018835:Chaperonin 10 / Q000737:chemistry* / Q000378:metabolism; D018834:Chaperonin 60 / Q000737:chemistry / Q000378:metabolism*; D017124:Conserved Sequence; D016208:Databases, Factual; D009682:Magnetic Resonance Spectroscopy; D008854:Microscopy, Electron; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry; D017550:Spectroscopy, Fourier Transform Infrared
D018835:Chaperonin 10; D018834:Chaperonin 60; D011994:Recombinant Proteins