Prediction of the structure of GroES and its interaction with GroEL

Proteins. 1995 Jul;22(3):199-209. doi: 10.1002/prot.340220302.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Chaperonin 10 / chemistry*
  • Chaperonin 10 / metabolism
  • Chaperonin 60 / chemistry
  • Chaperonin 60 / metabolism*
  • Conserved Sequence
  • Databases, Factual
  • Magnetic Resonance Spectroscopy
  • Microscopy, Electron
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation / genetics
  • Protein Conformation*
  • Protein Folding
  • Protein Structure, Secondary
  • Recombinant Proteins / chemistry
  • Spectroscopy, Fourier Transform Infrared

Substances

  • Chaperonin 10
  • Chaperonin 60
  • Recombinant Proteins