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Related Experiment Videos

Conformational changes in the GroEL oligomer during the functional cycle

O Llorca1, S Marco, J L Carrascosa

  • 1Centro Nacional de Biotecnología, CSIC, Campus Universidad Autónoma de Madrid, Spain.

Journal of Structural Biology
|February 1, 1997
PubMed
Summary

GroEL chaperonin undergoes significant conformational changes upon binding nucleotides like ATP and cochaperonin GroES. These structural shifts, visualized by electron microscopy, are crucial for its protein folding cycle mechanism.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • GroEL is a molecular chaperone essential for protein folding.
  • Nucleotide binding and cochaperonin GroES interaction induce allosteric conformational changes in GroEL.

Purpose of the Study:

  • To investigate the conformational states of GroEL and GroEL-GroES complexes.
  • To elucidate the structural basis of GroEL's allosteric mechanism.

Main Methods:

  • Electron microscopy (EM) and image processing.
  • Analysis of GroEL and GroEL-GroES complexes with various nucleotides (ADP, ATP, AMP-PNP, ATPγS).
  • High-resolution structural determination (20-25 Å).

Main Results:

  • ATP and AMP-PNP binding induce similar conformational shifts in GroEL's apical domains.

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  • Distinct conformational states (TT, TR, RR) were resolved, showing asymmetric changes in the RR state.
  • Conformational changes persist after ATP hydrolysis when ADP and Pi are bound.

    • Conclusions:

    • GroEL undergoes significant conformational changes upon nucleotide and GroES binding.
    • These dynamic structural alterations are key to the GroEL-mediated protein folding cycle.
    • The study provides insights into the allosteric mechanism of GroEL.