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GroEL/GroES: structure and function of a two-stroke folding machine.

Z Xu1, P B Sigler

  • 1Department of Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, Yale University, 260 Whitney Avenue, New Haven, Connecticut, 06520-8114, USA.

Journal of Structural Biology
|March 2, 1999
PubMed
Summary
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Chaperonins like E. coli GroEL assist protein folding by releasing nonnative polypeptides into a hydrophilic chamber. This cycle, using ATP, facilitates proper protein structure formation, sometimes requiring multiple rounds for complex proteins.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • Chaperonins (Cpn60) are crucial for protein folding, a key step in gene expression.
  • The Escherichia coli GroEL chaperonin possesses a double-toroid structure facilitating substrate binding and conformational changes.

Purpose of the Study:

  • To elucidate the mechanism of chaperonins in mediating protein folding.
  • To detail the structural and functional roles of GroEL and GroES in the protein folding process.

Main Methods:

  • Structural and functional studies of the GroEL/GroES chaperonin system.
  • Analysis of ATP binding, hydrolysis, and conformational changes within the GroEL complex.

Main Results:

  • GroEL binds nonnative polypeptides in its hydrophobic cavity.

Related Experiment Videos

  • ATP and GroES binding induces conformational changes, releasing substrate into a hydrophilic chamber for folding.
  • A cyclical, opposing ring mechanism facilitates substrate loading and product release, consuming ATP.

    • Conclusions:

    • The GroEL/GroES system employs a sophisticated mechanism involving conformational changes and ATP hydrolysis to assist protein folding.
    • Each folding cycle provides a limited time (15s) for protein folding, with some proteins requiring multiple cycles for native state attainment.