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Related Experiment Videos

Crystal structure of the lambda repressor C-terminal domain octamer.

C E Bell1, M Lewis

  • 1The Johnson Foundation and Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, 37th and Hamilton Walk, Philadelphia, 19102-6059, USA.

Journal of Molecular Biology
|December 18, 2001
PubMed
Summary

The lambda repressor C-terminal domain (CTD) structure reveals a tetramer that can form an octamer. Specific residues at the tetramer interface are key to octamer formation, offering insights for protein engineering.

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Area of Science:

  • Structural biology
  • Molecular genetics
  • Biochemistry

Background:

  • The lambda repressor C-terminal domain (CTD) plays a crucial role in DNA binding and gene regulation.
  • Previous studies determined the CTD structure as a tetramer, proposing a model for octamer formation.
  • Understanding the precise structural basis of repressor oligomerization is essential for deciphering gene control mechanisms.

Purpose of the Study:

  • To elucidate the three-dimensional structure of the lambda repressor CTD under various conditions.
  • To confirm the tetrameric structure and investigate the formation of the octameric repressor.
  • To identify specific residues involved in tetramer-tetramer interactions within the octamer.

Main Methods:

  • X-ray crystallography was employed to determine the atomic resolution structures of the lambda repressor CTD.

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  • Multiple crystal forms were analyzed under diverse experimental conditions.
  • Structural comparison and analysis of protein-protein interfaces were performed.

    • Main Results:

    • The lambda repressor CTD consistently forms a 2-fold symmetric tetramer across different crystal forms.
    • A crystal structure revealed an octameric complex, consistent with the previously proposed model.
    • Unique interactions involving Gln209, Tyr210, and Pro211 were identified at the tetramer-tetramer interface, distinct from dimer-dimer interactions.

    Conclusions:

    • The lambda repressor CTD exists as a stable tetramer, capable of forming an octamer.
    • Specific amino acid residues at the tetramer interface are critical for octamer assembly.
    • Targeted mutations at these identified residues could potentially yield repressors that form tetramers but not octamers, offering a route for protein engineering.