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Related Experiment Videos

Unliganded GroEL at 2.8 A: structure and functional implications

P B Sigler1, A L Horwich

  • 1Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06510, USA.

Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
|April 29, 1995
PubMed
Summary
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The structure of E. coli GroEL chaperonin reveals its two rings and central channel. This provides a framework for understanding how GroEL assists protein folding.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • The E. coli chaperonin GroEL is essential for protein folding.
  • Understanding GroEL's structure is key to elucidating its function.

Purpose of the Study:

  • To determine the three-dimensional structure of E. coli GroEL.
  • To provide a structural basis for interpreting biochemical and mutagenesis studies of GroEL.

Main Methods:

  • X-ray crystallography was used to determine the structure.
  • Refinement was performed to 2.7 A resolution in two crystal forms (orthorhombic and monoclinic).

Main Results:

  • The structure of GroEL was determined in ligand-free and ATP-analogue liganded states.

Related Experiment Videos

  • GroEL forms a 146 A high cylinder with two sevenfold symmetric rings.
  • Each ring consists of 7 identical subunits, each with three distinct domains: equatorial, apical, and intermediate.

    • Conclusions:

    • The determined structures offer a scaffold for interpreting functional studies.
    • The structural details highlight potential mechanisms for substrate binding and allosteric regulation.